Methods for immunoregulation by modulating plasminogen-apple-nematode (pan) domain-containing proteins

ABSTRACT

The present disclosure based on the inventors&#39; recognition that PAN domain containing proteins play important immune regulating functions. Disclosed herein are methods for modulating immune responses in plants and animals, improving in vitro fertilization efficiency, and inhibiting human cell division and cellular migration in cancer cells. Also disclosed herein are genetically modified plants that are resistant to pathogenic infections.

CROSS REFERENCE T0 RELATED APPLICATION

This application claims the benefit of priority from U.S. ProvisionalApplication No. 62/896,605, filed Sep. 6, 2019, the entire contents ofwhich are incorporated herein by reference.

STATEMENT REGARDING FEDERALLY SPONSORED RESEARCH OR DEVELOPMENT

This disclosure was made with government support under a researchproject supported by Prime Contract No. DE-AC05-000R22725 awarded by theU.S. Department of Energy. The government has certain rights in thisinvention.

INCORPORATION BY REFERENCE OF SEQUENCE LISTING

The Sequence Listing in an ASCII text file, named as38529Seglist_ST25.txt of 49 KB, created on Sep. 1, 2020, and submittedto the United States Patent and Trademark Office via EFS-Web, isincorporated herein by reference.

BACKGROUND

Immunoregulation (e.g. immunosuppression) is an essential phenomenongoverning fertilization during sexual reproduction, cell growth andproliferation as well as recruitment of beneficial symbionts. However,the same phenomenon predisposes host organisms to uncontrolled cellgrowth and infection by parasites, pathogens, and viruses. Consequently,understanding the molecular basis of immunoregulation (e.g.,immunosuppression or immunostimulation) has broad implications.

The Plasminogen-Apple-Nematode (PAN) domain (IPR003609) was firstcharacterized by Tordai et al., (FEBS Letters, 461(1-2), 63-67, (1999))in which they noted that the domain was shared by theplasminogen/hepatocyte growth factor protein family, theprekallikrein/coagulation factor XI protein family and nematodeproteins. The domain possesses the characteristic 6-cysteine residues inits core that are highly conserved. These cysteine residues coordinatethree disulfide bridges to form a hair-pin loop structure.

Plasma kallikrein (EC 3.4.21.34) and coagulation factor XI (EC3.4.21.27) are two related plasma serine proteases activated by factorXIIA and which share the same domain topology: an N-terminal region thatcontains four tandem repeats of about 90 amino acids and a C-terminalcatalytic domain. The 90 amino-acid repeated domain contains 6 conservedcysteines. Three disulfide bonds link the first and sixth, second andfifth, and third and fourth cysteines. The domain can be drawn in theshape of an apple and has been accordingly called the “apple domain”.

The apple domains of plasma prekallikrein are known to mediate itsbinding to high molecular weight kininogen, the apple domains of factorXI bind to factor XIIa, platelets, kininogen, factor IX and heparin.

The apple domains display some sequence similarity with the N domain ofplasminogen/hepatocyte growth factor (HGF) and to some nematode andprotozoan proteins. They all belong to the same domain superfamily thathave been called the PAN module. The N domain of hepatocyte growthfactor binds to the c-Met receptor and to the heparin molecule. Thestructure of the PAN module of HGF has been solved. It contains acharacteristic hairpin-loop structure stabilised by two disulfidebridges, Cys-1 and 6 are not conserved in HGF PAN modules.

Apart from the cysteines, there are a number of other conservedpositions in the apple domain. The PAN domain is thought to mediateprotein-protein or carbohydrate-protein interactions and facilitatereceptor dimerization.

Immunoregulation has been well recorded in plants. Plasma membrane boundpattern recognition receptors (PRR) are integral part of surveillancesystem against pathogens. Among the PRR which has a receptor kinasedomain are known as receptor kinases. These receptor kinases are furtherclassified into specific sub-types including Lectin-rich receptorkinases (L-type RLKs). L-type RLKs are well known for their role intriggering plant defense responses upon pathogen invasion. In contrast,it has been shown that a different class of receptor kinases, the PANdomain-containing D-mannose lectin binding domain receptor-like proteinkinases (G-type RLKs), function to suppress defense response in plants.G-type RLKs were shown to function as negative regulators of defensesignaling during pathogenesis by the fungal pathogen Sphaerulina musiva,parasitism of Arabidopsis by nematodes, and conversion of Arabidopsisinto a host of the fungal symbiont Laccaria bicolor. Moreover, PANdomain carrying S-locus kinases, reported to mediateself-incompatibility during pollination, fall under the same class ofG-LecRLKs. However, the specific role of the PAN domain in all theseprocesses has not been fully described.

In animal systems, PAN domain proteins function in cell growth andproliferation. One example is the Hepatocyte growth factor (HGF) whichhas a similar domain structure with N terminal PAN domain, multiplekringle domain and a serine protease domain. HGF consists ofcharacteristic heterodimer connected by a disulfide bond. HGF acts as animportant paracrine mediator of growth, invasion and angiogenesis inseveral cancers. All biological impacts of HGF are triggered bystimulating its cell surface receptor. Both high and low affinityreceptors have been identified for HGF. The high affinity receptor c-METproto-oncogene is a receptor tyrosine kinase that is turned on by HGFligand binding leading to a series of phosphorylation events includingSTAT3 phosphorylation, eventually turning on the HGF/c-MET signalingcascade. Hyperactivation of HGF/c-MET for instance, has been reported inlung cancer, colorectal cancer, glioblastoma, acute myeloid lymphomaamong others with higher mortality rate. Recent evidence suggests thatHGF can confer significant resistance to targeted cancer drugs includingmultiple kinase inhibitors interfering with current anti-cancer effort.

However, HGF/c-MET signaling is a key step for embryogenesis and tissueregeneration in the adult life which suggests a strict regulatorymechanism is important to determine the fate of the cells from a healthyone to tumorigenic. Recently, HGF/MET pathway emerged as a key targetfor anti-cancer therapy, although the major problem associated withsmall molecule inhibitors of MET and anti HGF-antibodies is that most ofthem are unstable and expensive. Although the interaction between METand HGF were well studied, it was not clear which amino acids in α-chainof HGF serve as the binding region for cMET receptor.

SUMMARY OF THE DISCLOSURE

In one aspect the disclosure is directed to a method for screening foran immunoregulatory protein comprising assessing the sequence of acandidate protein, and determining that the candidate protein is animmunoregulatory protein when at least one Plasminogen Apple Nematode(PAN) domain is found in the sequence.

In some embodiments, the PAN domain has a consensus sequence as shown inSEQ ID NO: 23.

Another aspect of the disclosure is directed to a method for screeningfor a therapeutic compound targeting a PAN domain in a protein,comprising contacting the protein comprising the PAN domain with acandidate therapeutic compound, and assessing whether the compound bindsto the PAN domain.

In some embodiments, the PAN domain-containing protein is selected fromproteins listed in List 1.

Another aspect of the disclosure is directed to a method for screeningfor a MET signaling inhibitor, comprising expressing a c-MET receptor onthe surface of a cell; incubating the cell with Hepatocyte Growth Factor(HGF) in the presence of a candidate inhibitor of PAN domaininteractions; and determining that the candidate inhibitor is aninhibitor of c-MET signaling if the interaction with c-MET and HGF isinhibited.

In some embodiments, the candidate inhibitor of PAN domain interactionsis a peptide comprising a consensus sequence as shown in SEQ ID NO: 23.In some embodiments, the candidate inhibitor of PAN domain interactionsis a small molecule.

Another aspect of the disclosure is directed to a method for enhancingimmune response to a pathogen in a plant comprising inactivating a geneencoding a PAN domain-containing protein in the plant. In someembodiments, the inactivating is achieved by introducing a non-silentmutation in the gene at a position encoding a conserved cysteine residueof the PAN domain. In some embodiments, the PAN domain-containingprotein is selected from plant G-type receptor-like protein kinases. Insome embodiments, the conserved cysteine residue is selected from aresidue equivalent to a cysteine at position 1, 32, 36, 40, 42, or 57 ofSEQ ID NO: 25.

In some embodiments, the non-silent mutation is a nonconservativemutation. In some embodiments, the nonconservative mutation is acysteine to alanine mutation.

In some embodiments, the inactivating of the gene encoding a PANdomain-containing protein is achieved by introducing an exogenousnucleic acid inhibitor of the gene to the plant. In some embodiments,the nucleic acid inhibitor is selected from the group consisting of anantisense RNA, a small interfering RNA, an RNAi, a microRNA, anartificial microRNA, and a ribozyme.

In some embodiments, the inactivating of the selected gene is achievedby genome editing, which is achieved by a method selected from the groupconsisting of CRISPR/Cas system, Cre/Lox system, TALEN system, ZFNssystem and homologous recombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the plant a first nucleic acid encoding a Cas9nuclease, a second nucleic acid comprising a guide RNA (gRNA), whereinsaid gRNA is specific to the gene encoding a PAN domain containingprotein.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the plant a first nucleic acid encoding a Cas9nuclease, a second nucleic acid comprising a guide RNA (gRNA), whereinsaid gRNA is specific to the gene encoding a PAN domain containingprotein gene, and a third nucleic acid comprising a template forhomologous recombination.

In some embodiments, the pathogen is selected from a bacterium, a virusor a fungus.

Another aspect of the disclosure I directed to a genetically engineeredplant, wherein an endogenous gene encoding a PAN domain-containingprotein has been inactivated as a result of a genetic modification.

In some embodiments, the inactivating is achieved by introducing anon-silent mutation in the gene at a residue encoding a conservedcysteine residue of the PAN domain.

In some embodiments, the PAN domain-containing protein is selected fromG-type receptor-like protein kinases. In some embodiments, the conservedcysteine residue is selected from a residue equivalent to a cysteine atposition 1, 32, 36, 40, 42, or 57 of SEQ ID NO: 25.

In some embodiments, the non-silent mutation is a nonconservativemutation. In some embodiments, the nonconservative mutation is acysteine to alanine mutation.

Another aspect of the disclosure is directed to a method for preventingcell division of a human cell comprising inactivating a gene encoding aPAN domain containing protein in the human cell. In some embodiments,the inactivating is achieved by introducing a non-silent mutation in thegene at a residue encoding a conserved cysteine residue of the PANdomain.

In some embodiments, the PAN domain containing protein gene isHepatocyte Growth Factor (HGF).

In some embodiments, the conserved cysteine residue is selected from aresidue equivalent to a cysteine at position 34, 38, 48, or 60 of SEQ IDNO: 32.

In some embodiments, the non-silent mutation is a nonconservativemutation. In some embodiments, the nonconservative mutation is acysteine to alanine mutation.

In some embodiments, the inactivating of the gene encoding a PANdomain-containing protein is achieved by introducing an exogenousnucleic acid inhibitor of the gene to the cancer cell.

In some embodiments, the nucleic acid inhibitor is selected from thegroup consisting of an antisense RNA, a small interfering RNA, an RNAi,a microRNA, an artificial microRNA, and a ribozyme.

In some embodiments, the inactivating of the gene encoding a PANdomain-containing protein is achieved by genome editing, which isachieved by a method selected from the group consisting of CRISPR/Cassystem, Cre/Lox system, TALEN system, ZFNs system and homologousrecombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the cancer cell a first nucleic acid encoding a Cas9nuclease, and a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the gene encoding a PAN domaincontaining protein.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the cancer cell a first nucleic acid encoding a Cas9nuclease, a second nucleic acid comprising a guide RNA (gRNA), whereinsaid gRNA is specific to the gene encoding a PAN domain containingprotein, and a third nucleic acid comprising a template for homologousrecombination.

Another aspect of the disclosure is directed to a method for improvingin vitro fertilization (IVF) efficiency in a non-human subject sufferingfrom infertility comprising determining the sequence of a gene thatencodes a PAN domain-containing protein, and obtaining an ovum or asperm from the subject when a mutation is found in a conserved cysteineof the PAN domain of the PAN domain-containing protein, correcting themutation in the PAN domain-containing protein in the ovum or the sperm.

In some embodiments, the PAN domain-containing protein gene is a ZonaPellicuda(ZP) protein.

In some embodiments, wherein the conserved cysteine residue is selectedfrom a residue equivalent to a cysteine residue in SEQ ID NO: 23.

In some embodiments, the correcting of the PAN domain is achieved bygenome editing, which is achieved by a method selected from the groupconsisting of CRISPR/Cas system, Cre/Lox system, TALEN system, ZFNssystem and homologous recombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the ovum or the sperm a first nucleic acid encoding aCas9 nuclease, a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the gene encoding a PANdomain-containing protein, and a third nucleic acid comprising atemplate for homologous recombination that corrects the mutated residueto cysteine.

In some embodiments, the ovum or the sperm is from a domesticatedanimal.

Another aspect of the disclosure is directed to a method for preventingpregnancy or implantation of a fetus in a non-human subject comprisinginactivating a gene encoding a PAN domain-containing protein in an ovumor a sperm.

In some embodiments, the inactivating is achieved by introducing anon-silent mutation in the gene at a residue encoding a conservedcysteine residue of the PAN domain.

In some embodiments, the PAN domain containing protein gene is a ZonaPellicuda protein.

In some embodiments, the conserved cysteine residue is selected from aresidue equivalent to a cysteine a cysteine residue in SEQ ID NO: 23.

In some embodiments, the non-silent mutation is a nonconservativemutation. In some embodiments, the nonconservative mutation is acysteine to alanine mutation.

In some embodiments, the inactivating of the gene encoding a PANdomain-containing protein is achieved by introducing an exogenousnucleic acid inhibitor of the gene to the ovum or the sperm. In someembodiments, the nucleic acid inhibitor is selected from the groupconsisting of an antisense RNA, a small interfering RNA, an RNAi, amicroRNA, an artificial microRNA, and a ribozyme.

In some embodiments, the inactivating of the gene encoding a PANdomain-containing protein is achieved by genome editing, which isachieved by a method selected from the group consisting of CRISPR/Cassystem, Cre/Lox system, TALEN system, ZFNs system and homologousrecombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the ovum or the sperm a first nucleic acid encoding aCas9 nuclease, a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the gene encoding a PANdomain-containing protein.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the ovum or the sperm a first nucleic acid encoding aCas9 nuclease, a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the selected gene, and a third nucleicacid comprising a template for homologous recombination.

In some embodiments, the ovum or the sperm is from a domesticatedanimal.

Another aspect of the disclosure is directed to a method for screeningfor an oncoprotein protein in a mammalian cell comprising assessing thesequence of a candidate protein, and determining that the candidateprotein is an oncoprotein when at least one Plasminogen Apple Nematode(PAN) domain is found in the sequence.

In some embodiments, the PAN domain has a consensus sequence as shown inSEQ ID NO: 23.

Another aspect of the disclosure is directed to a method forinactivating a PAN domain-containing protein comprising introducing anon-silent mutation in the protein at a residue encoding a conservedcysteine residue of the PAN domain.

In some embodiments, the PAN domain-containing protein is selected fromproteins listed in List 1.

In some embodiments, the conserved cysteine residue is selected from aresidue equivalent to a cysteine residue in SEQ ID NO: 23.

BRIEF DESCRIPTION OF THE DRAWINGS

The patent or application file contains at least one drawing executed incolor. Copies of this patent or patent application publication withcolor drawing(s) will be provided by the Office upon request and paymentof the necessary fee.

FIG. 1. Amino acid conservation within different G-LecRK PAN domains andnaturally occurring variation in non-immunosuppressive Salix orthologsSapurV1A.0037s0270.1 and SapurV1A.0918s0020. The aligned PAN domains arethe following: SapurV1A.0387s0100.1 (SEQ ID NO: 24),SapurV1A.1175s0020.1 (SEQ ID NO: 25), SapurV1A.0037s0270.1 (SEQ ID NO:26), SapurV1A.1316s0010.1 (SEQ ID NO: 27), SapurV1A.0918s0020.1 (SEQ IDNO: 28), AT1G61380 (SEQ ID NO: 29), Potri.005G018000.1 (SEQ ID NO: 30),Potri.T022200.1 (SEQ ID NO: 31).

FIG. 2. Domain architecture of PAN domain proteins in Anopheles gambiaeand Diaphorina citri.

FIG. 3. Proportion of protein domains co-occurring with the PAN domainin Fusarium oxysporum species complex.

FIGS. 4A-4B. Proportion of protein domain co-occurring with the PANdomain in oomycetes Aphanomyces astaci and Phytophthora ramorum.

FIGS. 5A-5B. Tandem expansion of G-LecRKs (orange blocks) on chromosome4 and 9 of Oryza sativa compared to the syntenic region in the Oryzapunctata genome.

FIGS. 6A-6K. Protein domain co-occurring with the PAN domain acrossorganismal categories. (A) Alveolata, (B) Amoebozoa, (C) Archea, (D)Bacteria, (E) Cryptophyta; (F) Euglenozoa, (G) Haptophyceae, (H) MetaGenomics, (I) Opisthokonka, (J) Stramenoplies, (K) Viridplantae.

FIG. 7. Domain composition of PAN domain-containing proteins in viruses.

FIG. 8. Amino acid conservation within the PAN domain in different humanproteins. NM_000601.5 represents HGF. Arrows show the four conservedCysteine (C) and one conserved Asparagine (N). PAN domains used in thealignment are from the following proteins: NM_000601.5 (SEQ ID NO: 32);NP_001258662.1 (SEQ ID NO: 33); XP_016861955.1 (SEQ ID NO: 34);XP_016861956.1 (SEQ ID NO: 35); NP_066278.3 (SEQ ID NO: 36);XP_016861952.1 (SEQ ID NO: 37); XP_011532040.1 (SEQ ID NO: 38);XP_016861957.1 (SEQ ID NO: 39); XP_016861954.1 (SEQ ID NO: 40);XP_016861953.1 (SEQ ID NO: 41); XP_016861949.1 (SEQ ID NO: 42);XP_016861950.1 (SEQ ID NO: 43); XP_016861951.1 (SEQ ID NO: 44);XP_006713229.1 (SEQ ID NO: 45); XP_011532034.1 (SEQ ID NO: 46).

FIG. 9. Conserved cysteine residues in HGF-PAN domain are essential forHGF/c-MET signaling.

FIG. 10. Mutating cysteine residues in HGF results in enhanced proteinstability and attenuation of c-MET signaling.

FIG. 11. Schematic representation of the impact of wild type and PANmutant HGF on c-MET signaling. Wild type HGF can bind with c-METreceptor on the cell membrane and turn on the subsequent signalingcascade whereas the PAN mutant HGF cannot.

FIGS. 12A-12B. (A) Disruption of homodimerization by minimal mutationsin the PAN domain of RLK5 protein. (B) Restoration of PAN amino acids toconsensus sequence enhances RLK5R homodimerization.

FIGS. 13A-13B. (A) A functional PAN domain enhances receptor proteolysis(RLK7R) whereas minimal mutations in the PAN domain enhance RLK7stability. (B) Additionally, receptor proteolysis retards MPK3 and 6expression in RLK7R transgenic lines while the stable RLK7 exhibitsinduction of both MPK3 and MPK6.

FIGS. 14A-14C. Transcriptional activation of MAP kinases in Arabidopsistransgenic lines overexpressing RLK5 and 7. RLK25 is an L-type RLK thatfunctions as positive defense regulator. (A) MAPKKK13; (B) MAPKKK14; (C)MPK3.

FIGS. 15A-15F. Transcriptional activation of jasmonic acid and ethylenedefense marker genes in Arabidopsis transgenic lines overexpressing RLK5and 7. RLK25 is an L-type RLK that functions as positive defenseregulator. (A) JAZ5, (B) LOX4, (C) ERF13, (D) ACS11, (E) ACS7, (F) LOX3.

FIGS. 16A-16B. Transcriptional activation of jasmonic acid and ethylenedefense marker genes in Arabidopsis transgenic lines overexpressing RLK5and 7. RLK25 is an L-type RLK that functions as positive defenseregulator. (A) PR1; (B) NPR3.

FIGS. 17A-17C. Transcriptional activation of canonical defense-relatedWRKY transcriptional factors in Arabidopsis transgenic linesoverexpressing RLK5 and 7. RLK25 is an L-type RLK that functions aspositive defense regulator. (A) WRKY18; (B) WRK33; (C) WRKY40.

FIG. 18. Proposed model showing RLKs with mutated PAN domainsspecifically activate ET/JA pathway and attenuates SA and ABA pathway inplant innate immunity. Scheme of activation of JA and ET pathway in RLKPAN overexpressed transgenic pant in Arabidopsis. The green arrowindicates upregulation, and the red arrow indicates the downregulation.These results suggest that RLK PAN transgenic plants shows activatedET/JA pathway and attenuated SA and ABA signaling pathway.

FIG. 19. HGF PAN mutants inactivate MAPK and AKT signaling in HEK293Tcells.

FIG. 20. HGF PAN mutants downregulate the activation of cMET signalingcascade in glioblastoma cell line U87.

FIG. 21. Cell proliferation following HGF stimulations in cell HEK 293Tcells. Cells show higher absorbance at 24 and 48 hr following WT HGFstimulation compared to 4Cys-4Ala HGF.

FIGS. 22A-22E. Expression of (A) cMET and (B) MMP9 in HEK 293T cellsupon HGF stimulation as determined by real time quantitative PCR.Expression of (C) cMET, (D) MMP9 and (E) MMP2 in U87 cells upon HGFstimulation as determined by real time quantitative PCR.

DETAILED DESCRIPTION Definitions

As used herein, the phrase “immunoregulatory protein” or “immuneregulatory protein” refers to a protein that regulates a cell's responseto a foreign entity. In some embodiments, an immunoregulatory proteinsuppresses the ability of a cell to respond to the foreign entity (i.e.,it is an “immunosuppressor”). The cell can be an animal cell, a plantcell, a fungal cell, or a bacterial cell. In some embodiments, animmunoregulatory protein increases or enables the ability of a cell torespond to the foreign entity (i.e., it is an “immunostimulant”). Theability of a cell to respond to a foreign entity refers to, for example,binding to a foreing entity triggering signaling within the cell thatleads to, for example, release of a defensive substance (e.g., acytokine, an antibacterial or antiviral substance) or rejection of theforeign entity. Overexpression of an immunosuppressor immunoregulatoryprotein in a cell suppresses/inhibits the cell's immune response to aforeign entity apart and independent of the general immune system of theorganism to which the cell belongs. Overexpression of animmunostilmulant immunoregulatory protein in a cell potentiates thecell's immune response to a foreign entity apart and independent of thegeneral immune system of the organism. For example, the inventors havediscovered that overexpressing two Salix purpurea G-LecRKs (PAN domaincontaining proteins) (SapurV1A.0037s0270.1 and SapurV1A.0918s0020)stimulate immune responses in Arabidopsis cells, whereas overexpressinothr G-LecRKs (e.g., SapurV1A.0387s0100.1, SapurV1A.1175s0020.1, andSapurV1A.1316s0010.1) suppress immune responses in Arabidopsis cells.

The term “homolog” or “homologous” means a gene related to a second geneby descent from a common ancestral DNA sequence, therefore, thecorresponding polynucleotide/polypeptide has a certain degree ofhomology, i.e., sequence identity (at least 40%, 60%, 65%, at least 66%,68%, 70%, 75%, 80%, 86%, 88%, 90%, 92%, 95%, 97% or 99% sequenceidentity). A “homolog” furthermore means that the function is equivalentto the function of the original gene. Homologs of a given gene andcorresponding or equivalent positions in the homologous genes orproteins can be determined by sequence alignment programs, e.g.,including but not limited to, NCBI BLAST, ClustalW, DIAMOND, CS-BLAST,and MAFFT. For example, an alignment of PAN domains ofSapurV1A.0387s0100.1 (SEQ ID NO: 24), SapurV1A.1175s0020.1 (SEQ ID NO:25), SapurV1A.0037s0270.1 (SEQ ID NO: 26), SapurV1A.1316s0010.1 (SEQ IDNO: 27), SapurV1A.0918s0020.1 (SEQ ID NO: 28), AT1G61380 (SEQ ID NO:29), Potri.005G018000.1 (SEQ ID NO: 30), and Potri.T022200.1 (SEQ ID NO:31) is shown in FIG. 1. The alignment shows that while the conservedcysteine residues in SapurV1A.1175s0020.1 are at positions 1, 32, 36,40, 42, and 57 of SEQ ID NO: 25, corresponding/equivalent conservedcysteine residues in SapurV1A.0387s0100.1 are at positions 1, 39, 43,47, 49 and 60 of SEQ ID NO: 24.

As used herein, the phrase “nonconservative mutation” refers to a changein a DNA or RNA sequence that results in the replacement of an aminoacid with one that is not biochemically similar. In some embodiments, anonconservative mutation of a cysteine residue is a changing thesysteine residue to any amino acid other than serine, selenocysteine,threonine, and methionine (because serine, selenocysteine, threonine,and methionine are biochemically similar to cysteine).

The term “small molecule compound” herein refers to small organicchemical compound, generally having a molecular weight of less than 2000daltons, 1500 daltons, 1000 daltons, 800 daltons, or 600 daltons.

Targeted Genome Engineering

Targeted genome engineering (also known as genome editing) has emergedas an alternative to classical plant breeding and transgenic(Genetically Modified Organism—GMO) methods to improve crop plants.Available methods for introducing site-specific double strand DNA breaksinclude zinc finger nucleases (ZFNs), TAL effector nucleases (TALENs)and CRISPR/Cas system. ZFNs are reviewed in Carroll, D. (Genetics, 188.4(2011): 773-782), and TALENs are reviewed in Zhang et al. (PlantPhysiology, 161.1 (2013): 20-27), which are incorporated herein in theirentirety.

CRISPR/Cas system is a method based on the bacterial type II CRISPR(clustered regularly interspaced short palindromic repeats)/Cas(CRISPR-associated) immune system. The CRISPR/Cas system allows targetedcleavage of genomic DNA guided by a customizable small noncoding RNA,resulting in gene modifications by both non-homologous end joining(NHEJ) and homology-directed repair (HDR) mechanisms. Belhaj et al.(Plant Methods, 2013, 9:39) summarizes and discusses applications of theCRISPR/Cas technology in plants and is incorporated herein in itsentirety.

In a specific embodiment genome editing is achieved by CRISPR (Clusteredregularly-interspaced short palindromic repeats)/Cas technology.CRISPR-Cas and similar gene targeting systems are well known in the artwith reagents and protocols readily available. Exemplary genome editingprotocols are described in Jennifer Doudna, and Prashant Mali,“CRISPR-Cas: A Laboratory Manual” (2016) (CSHL Press, ISBN:978-1-621821-30-4) and Ran, F. Ann, et al. (Nature Protocols (2013), 8(11): 2281-2308).

In a specific embodiment, CRISPR-mediated gene repair comprisesintroducing said plant a first nucleic acid encoding a wild type Cas9nuclease, a second nucleic acid comprising a guide RNA (gRNA) specificfor targeting the mutated genomic region and a third nucleic acidcomprising a homologous repair template (aka. Homology DirectedRepair—HDR template) of said RLP1, RLP2, L-type lecRLK genes with saiddeleterious mutation. In this embodiment, the specific guide RNA targetsthe Cas9 nuclease to the mutated genomic region and the Cas9 nucleaseintroduces a double strand break in the targeted DNA region. In thepresence of the homology template which contains a substantiallyfunctional copy of the mutated genomic region (with the deleteriousmutation corrected), DNA repair mechanism favors Homology DirectedRepair (HDR) and the mutation in the targeted gene is corrected.

The Plasminogen Apple Nematode (PAN) Domain

The PAN domain (Pfam ID: PF00024; InterPro ID: IPR003609; PROSITE ID:PDOC00376) contains 4 to 6 conserved cysteine residues. The conservedresidues are involved in the formation of disulfide bond links betweenthe first and sixth, second and fifth, third and fourth cysteines toform a hairpin-loop structure. Cysteine residues 1 and 6 are notconserved in some PAN domain containing proteins such as the HepatocyteGrowth Factor (HGF). As used herein, a PAN domain has the followingconsensus sequence:C-x(3)-[LIVMFY]-x(5)-[LIVMFY]-x(3)-[DENQ]-[LIVMFY]-x(10)-C-x(3)-C-T-x(4)-C-x-[LIVMFY]-F-x-[FY]-x(13-14)-C-x-[LIVMFY]-[RK]-x-[ST]-x(14-15)-S-G-x-[ST]-[LIVMFY]-x(2)-C(SEQID NO: 23). In some embodiments, the consensus sequence has the sequenceas shown in any one of SEQ ID NO: 50-52. The skilled artisan candetermine whether a protein comprises a PAN domain by searching theamino acid sequence of the protein using the consensus PAN domainsequence as a query sequence and any sequence alignment software.

The inventors of the instant disclosure have curated >28,000 proteinsacross eukaryotes, archaea, bacteria and viruses carrying the PANdomain. See List 1. After classifying 2,496 organisms representing 959genera, into 13 categories (Alveolata, Archea, Amoebazoa, Bacteria,Cryptophyta, Euglenozoa, Haptophyceae, Opisthokonta, Rhizaria,Rhodophyta, Stramenopilles, Viridplantae, and Viruses) the inventorsobserved that proteins carrying the PAN domain have been implicated inmodulation of immune responses across divergent organisms (e.g., fromplants to animals, from viruses to bacteria and fungi), suggesting thatthe domain may have been co-opted to serve the same immunosuppressivefunction under different biological circumstances.

Methods for Screening for an Immunoregulatory Protein

The inventors of the instant disclosure have discovered that proteinsthat contain at least one PAN domain are involved in immunoregulation.In some embodiments, a PAN domain-containing protein functions as animmunosuppressor.

One aspect of the disclosure is directed to a method for screening foran immune regulating protein comprising assessing the sequence of acandidate protein, and determining that the candidate protein is animmune regulating protein when at least one Plasminogen Apple Nematode(PAN) domain is found in the sequence.

It has been found by the present inventors that a PAN domain is presentin proteins having an immunoregulatory function. For example, aGO-enrichment analysis by the present inventors using >28,000 PANdomain-containing proteins listed in List 1 revealed 39 GO-terms thatwere enriched at p<0.05. These included terms like cell recognition(p<1E-30), cell communication (p<1E-30), proteolysis (p<1E-30),pollen-pistil interaction (p<1E-30), reproduction (p<1E-30), response tostimulus (p<1E-30) and response to stress (p<1E-30). These processes areconsistent with roles in modulation of immune responses.

In some embodiments, the PAN domain has a consensus sequence as shown inSEQ ID NO: 23.

In some embodiments, the candidate protein is selected from a plantprotein, an animal protein, a bacterial protein, a viral protein and afungal protein. In some embodiments, the animal is a domesticated animal(cow, sheep, cat, dog, goat, etc) or a human.

In some embodiments, at least four conserved cysteine residues in thePAN domain of the immunoregulatory protein. In some embodiments, the atleast four conserved cysteine residues comprise cysteines correspondingto the second cysteine to the fifth cysteine of SEQ ID NO: 23. In someembodiments, all six cysteine residues that correspond to the sixcysteine residues of SEQ ID NO: 23 are conserved in the protein.

Methods for Screening for a Therapeutic Compound Targeting a PAN Domain

Another aspect of the disclosure is directed to a method for screeningfor a therapeutic compound targeting a PAN domain in a protein,comprising contacting the protein comprising the PAN domain with acandidate therapeutic compound, and assessing whether the compound bindsto the PAN domain.

In some embodiments, the candidate compound is a small moleculecompound.

In some embodiments, the candidate compound binds to the PAN domain witha KD of 10⁻⁷ M, 10⁻⁸ M, 10⁻⁹ M, 10⁻¹⁰ M, 10⁻¹¹ M, 10⁻¹² M or less.

In some embodiments, the binding affinity of the candidate compound ismeasured by a competitive binding assay.

In some embodiments, the PAN-domain containing protein is selected fromthe proteins listed in List 1.

In some embodiments, the PAN domain in the PAN domain containing proteinhas a consensus sequence as shown in SEQ ID NO: 23.

In some embodiments, the protein is selected from a plant protein, ananimal protein, a bacterial protein, a viral protein and a fungalprotein.

In some embodiments, a compound, which is identified as binding to thePAN domain, inhibits the immunoregulatory function of the PANdomain-containing protein. For example, hepatocyte growth factor (HGF),a PAN domain-containing protein, is an immunoregulator that acts throughits interaction with the cMET receptor. The inventors of the instantdisclosure have found that the PAN domain in HGF is critical for itsinteraction with cMET receptor and its role in immunoregulation.

Methods for Screening for a MET Signaling Inhibitor

A different aspect of the disclosure is directed to a method forscreening for a MET signaling inhibitor, comprising expressing a c-METreceptor on the surface of a cell; incubating the cell with HepatocyteGrowth Factor (HGF) in the presence of a candidate inhibitor of PANdomain interactions; and determining that the candidate inhibitor is aninhibitor of c-MET signaling if the interaction with c-MET and HGF isinhibited.

In some embodiments, the candidate inhibitor of PAN domain interactionsis a competitive inhibitor of PAN domain binding. In some embodiments,the candidate inhibitor of PAN domain interactions is an allostericinhibitor of PAN domain binding.

In some embodiments, the candidate inhibitor of PAN domain interactionsis a peptide comprising a consensus sequence as shown in SEQ ID NO: 23.

In some embodiments, the inhibitor candidate is a small moleculecompound.

In some embodiments, the inhibitor candidate binds to the PAN domainwith a KD of 10⁻⁷ M, 10⁻⁸ M, 10⁻⁹ M, 10⁻¹⁰ M, 10⁻¹ M, 10⁻¹ M or less.

In some embodiments, the cell is a mammalian cell.

Methods for Enhancing Immune Response to Pathogens in Plants

It has been found in accordance with this disclosure that PANdomain-containing proteins in plants have the function of suppressingthe plant immune response to foreign entities. While in some instancesthe foreign entity is a symbiont beneficial to the plant, in otherinstances the foreign entity is a pathogen.

Another aspect of the disclosure is directed to a method for enhancingimmune response or resistance to a pathogen in a plant comprisinginactivating a gene encoding a PAN domain-containing protein in theplant.

In some embodiments, the inactivating is achieved by introducing anon-silent mutation in the gene at a residue encoding a conservedcysteine residue of the PAN domain.

In some embodiments, the PAN domain containing protein gene is selectedfrom a plant G-type receptor-like protein kinase gene. In someembodiments, a G-type receptor-like protein kinase gene has a nucleotidesequence that is homologous to SEQ ID NO: 47. In some embodiments, aG-type receptor-like protein kinase gene has a nucleotide sequence thatis at least 70%, 73% 75%, 78%, 80%, 83%, 85%, 88%, 90%, 93%, 95% or 99%,or more identical to SEQ ID NO: 47. In some embodiments, a G-typereceptor-like protein kinase gene encodes a protein that has an aminoacid sequence that is homologous to SEQ ID NO: 48. In some embodiments,a G-type receptor-like protein kinase gene encodes a protein that has anamino acid sequence that is at least 70%, 73% 75%, 78%, 80%, 83%, 85%,88%, 90%, 93%, 95% or 99%, or more identical to SEQ ID NO: 48.

In some embodiments, the conserved cysteine residue is selected from aresidue equivalent to a cysteine at position 1, 32, 36, 40, 42, or 57 ofSEQ ID NO: 25.

In some embodiments, the non-silent mutation is a nonconservativemutation.

In some embodiments, the nonconservative mutation is a cysteine toalanine mutation.

In some embodiments, the inactivating of the gene encoding a PAN domaincontaining protein is achieved by introducing an exogenous nucleic acidinhibitor of the gene to the plant.

In some embodiments, the nucleic acid inhibitor is selected from thegroup consisting of an antisense RNA, a small interfering RNA, an RNAi,a microRNA, an artificial microRNA, and a ribozyme.

In some embodiments, the inactivating of the selected gene is achievedby genome editing, which is achieved by a method selected from the groupconsisting of CRISPR/Cas system, Cre/Lox system, TALEN system, ZFNssystem and homologous recombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the plant a first nucleic acid encoding a Cas9nuclease, a second nucleic acid comprising a guide RNA (gRNA), whereinsaid gRNA is specific to the gene encoding a PAN domain containingprotein.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the plant a first nucleic acid encoding a Cas9nuclease, a second nucleic acid comprising a guide RNA (gRNA), whereinsaid gRNA is specific to the gene encoding a PAN domain containingprotein, and a third nucleic acid comprising a template for homologousrecombination.

In some embodiments, the pathogen is selected from a bacterium, a virusor a fungus.

In some embodiments, the pathogen is a necrotropic fungus selected fromthe group consisting of Sphaerulina abeliceae, Sphaerulina aceris,Sphaerulina acetabulum, Sphaerulina acori, Sphaerulina aechmeae,Sphaerulina affinis, Sphaerulina albispiculata, Sphaerulina alni,Sphaerulina amelanchier, Sphaerulina amicta, Sphaerulina amphilomatis,Sphaerulina amygdali, Sphaerulina anemones, Sphaerulina annae,Sphaerulina antarctica, Sphaerulina arctica, Sphaerulina arthoniae,Sphaerulina assurgens, Sphaerulina aucubae, Sphaerulina azaleae,Sphaerulina baccarum, Sphaerulina bambusicola, Sphaerulina berberidis,Sphaerulina betulae, Sphaerulina blyttii, Sphaerulina bonariana,Sphaerulina boudieriana, Sphaerulina bryophila, Sphaerulina callista,Sphaerulina camelliae, Sphaerulina camelliae, Sphaerulina carestiae,Sphaerulina caricae, Sphaerulina caricis, Sphaerulina ceanothi,Sphaerulina centellae, Sphaerulina cercidis, Sphaerulina cetraricola,Sphaerulina cetrariicola, Sphaerulina chlorococca, Sphaerulina cibotii,Sphaerulina citri, Sphaerulina codiicola, Sphaerulina coffaeicola,Sphaerulina coffeicola, Sphaerulina concinna, Sphaerulina conflicta,Sphaerulina coriariae, Sphaerulina cornicola, Sphaerulina corniculata,Sphaerulina coronillae-junceae, Sphaerulina corynephora, Sphaerulinacucumeris, Sphaerulina cucurbitae, Sphaerulina datiscae, Sphaerulinadiapensiae, Sphaerulina dioscoreae, Sphaerulina divergens, Sphaerulinadolichotera, Sphaerulina dryadis, Sphaerulina dryophila, Sphaerulinadubiella, Sphaerulina empetri, Sphaerulina endococcoidea, Sphaerulinaepigaea, Sphaerulina eucalypti, Sphaerulina ferruginosa, Sphaerulinafrondicola, Sphaerulina fuegiana, Sphaerulina gei, Sphaerulinagentianae, Sphaerulina gigantea, Sphaerulina giliae, Sphaerulinahainensis, Sphaerulina halophila, Sphaerulina hamadryadum, Sphaerulinahederae, Sphaerulina helicicola, Sphaerulina hyperici, Sphaerulinainaequalis, Sphaerulina inquinans, Sphaerulina intermedia, Sphaerulinaintermixta, Sphaerulina ipomoeae, Sphaerulina islandica, Sphaerulinaiwatensis, Sphaerulina juglandis, Sphaerulina leightonii, Sphaerulinalepidiotae, Sphaerulina limnanthemi, Sphaerulina lini, Sphaerulinalinicola, Sphaerulina ludwigiae, Sphaerulina mappiae, Sphaerulinamarattiae, Sphaerulina marginata, Sphaerulina maroccana, Sphaerulinamarsileae, Sphaerulina maydis, Sphaerulina menispermi, Sphaerulinamicrothyrioides, Sphaerulina mimosae-pigrae, Sphaerulina miyakei,Sphaerulina musae, Sphaerulina muscicola, Sphaerulina muscorum,Sphaerulina musicola, Sphaerulina musiva, Sphaerulina myriadea,Sphaerulina myriadea subsp. myriadea, Sphaerulina myrtillina,Sphaerulina naumovii, Sphaerulina nephromiaria, Sphaerulina oleifolia,Sphaerulina orae-maris, Sphaerulina oryzae, Sphaerulina oryzina,Sphaerulina oxalidis, Sphaerulina oxyacanthae, Sphaerulina pallens,Sphaerulina parvipuncta, Sphaerulina patriniae, Sphaerulina paulistana,Sphaerulina peckii, Sphaerulina pedicellata, Sphaerulina pelargonii,Sphaerulina phalaenopsidis, Sphaerulina phellogena, Sphaerulinaphoenicis, Sphaerulina phyllostachydis, Sphaerulina pini, Sphaerulinaplantaginea, Sphaerulina pleuropogonis, Sphaerulina polygonorum,Sphaerulina polypodii, Sphaerulina polypodii, Sphaerulina polyspora,Sphaerulina populi, Sphaerulina populicola, Sphaerulina porothelia,Sphaerulina potebniae, Sphaerulina potentillae, Sphaerulina poterii,Sphaerulina primulicola, Sphaerulina pruni, Sphaerulinapseudovirgaureae, Sphaerulina pterocarpi, Sphaerulina pulii, Sphaerulinaquercicola, Sphaerulina quercifolia, Sphaerulina quitensis, Sphaerulinarehmiana, Sphaerulina rhabdoclinis, Sphaerulina rhodeae, Sphaerulinarhododendri, Sphaerulina rhododendricola, Sphaerulina rubi, Sphaerulinasaccardiana, Sphaerulina saccardoana, Sphaerulina sacchari, Sphaerulinasalicina, Sphaerulina sambucina, Sphaerulina sasae, Sphaerulinaschaereri, Sphaerulina scirpi, Sphaerulina sepincola, Sphaerulinaserograpta, Sphaerulina silacincola, Sphaerulina smilacincola,Sphaerulina socia, Sphaerulina spartii, Sphaerulina staphyleae,Sphaerulina staurochili, Sphaerulina steganostroma, Sphaerulina subgen.Pharcidiella, Sphaerulina subgen, Sphaerulina, Sphaerulina subglacialis,Sphaerulina subtropica, Sphaerulina suchumica, Sphaerulina tabacinae,Sphaerulina tanaceti, Sphaerulina tarda, Sphaerulina taxi, Sphaerulinataxicola, Sphaerulina thujopsidis, Sphaerulina tiliaris, Sphaerulinatirolensis, Sphaerulina todeae, Sphaerulina trapae-bispinosae,Sphaerulina trifolii, Sphaerulina tritici, Sphaerulina umbilicata,Sphaerulina valerianae, Sphaerulina viciae, Sphaerulina vincae,Sphaerulina violae, Sphaerulina vismiae, Sphaerulina vulpina,Sphaerulina westendorpii, Sphaerulina worsdellii, Sphaerulinaxerophylli, Sphaerulina yerbae, Sphaerulina ziziphi, Sphaerulinazizyphae, and Sphaerulina zizyphi.

Genetically-Engineered Plants Resistant to Pathogens and Parasites

Another aspect of the disclosure is directed to a genetically engineeredplant, wherein an endogenous gene encoding a PAN domain-containingprotein in the plant has been inactivated as a result of a geneticmodification.

In some embodiments, the inactivation is achieved by introducing anon-silent mutation in the gene at a residue encoding a conservedcysteine residue of the PAN domain.

In some embodiments, the gene encoding a PAN domain-containing proteinis selected from a plant G-type receptor-like protein kinase gene. Insome embodiments, a G-type receptor-like protein kinase gene has anucleotide sequence that is homologous to SEQ ID NO: 47. In someembodiments, a G-type receptor-like protein kinase gene has a nucleotidesequence that is at least 70%, 73% 75%, 78%, 80%, 83%, 85%, 88%, 90%,93%, 95% or 99%, or more identical to SEQ ID NO: 47. In someembodiments, a G-type receptor-like protein kinase gene encodes aprotein that has an amino acid sequence that is homologous to SEQ ID NO:48. In some embodiments, a G-type receptor-like protein kinase geneencodes a protein that has an amino acid sequence that is at least 70%,73% 75%, 78%, 80%, 83%, 85%, 88%, 90%, 93%, 95% or 99%, or moreidentical to SEQ ID NO: 48.

In some embodiments, the conserved cysteine residue is selected from aresidue equivalent to a cysteine at position 1, 32, 36, 40, 42, or 57 ofSEQ ID NO: 25.

In some embodiments, the non-silent mutation is a nonconservativemutation.

In some embodiments, the nonconservative mutation is a cysteine toalanine mutation.

In some embodiments, the pathogen is selected from a bacterium, a virusor a fungus.

In some embodiments, the pathogen is a necrotropic fungus selected fromthe group consisting of Sphaerulina abeliceae, Sphaerulina aceris,Sphaerulina acetabulum, Sphaerulina acori, Sphaerulina aechmeae,Sphaerulina affinis, Sphaerulina albispiculata, Sphaerulina alni,Sphaerulina amelanchier, Sphaerulina amicta, Sphaerulina amphilomatis,Sphaerulina amygdali, Sphaerulina anemones, Sphaerulina annae,Sphaerulina antarctica, Sphaerulina arctica, Sphaerulina arthoniae,Sphaerulina assurgens, Sphaerulina aucubae, Sphaerulina azaleae,Sphaerulina baccarum, Sphaerulina bambusicola, Sphaerulina berberidis,Sphaerulina betulae, Sphaerulina blyttii, Sphaerulina bonariana,Sphaerulina boudieriana, Sphaerulina bryophila, Sphaerulina callista,Sphaerulina camelliae, Sphaerulina camelliae, Sphaerulina carestiae,Sphaerulina caricae, Sphaerulina caricis, Sphaerulina ceanothi,Sphaerulina centellae, Sphaerulina cercidis, Sphaerulina cetraricola,Sphaerulina cetrariicola, Sphaerulina chlorococca, Sphaerulina cibotii,Sphaerulina citri, Sphaerulina codiicola, Sphaerulina coffaeicola,Sphaerulina coffeicola, Sphaerulina concinna, Sphaerulina conflicta,Sphaerulina coriariae, Sphaerulina cornicola, Sphaerulina corniculata,Sphaerulina coronillae-junceae, Sphaerulina corynephora, Sphaerulinacucumeris, Sphaerulina cucurbitae, Sphaerulina datiscae, Sphaerulinadiapensiae, Sphaerulina dioscoreae, Sphaerulina divergens, Sphaerulinadolichotera, Sphaerulina dryadis, Sphaerulina dryophila, Sphaerulinadubiella, Sphaerulina empetri, Sphaerulina endococcoidea, Sphaerulinaepigaea, Sphaerulina eucalypti, Sphaerulina ferruginosa, Sphaerulinafrondicola, Sphaerulina fuegiana, Sphaerulina gei, Sphaerulinagentianae, Sphaerulina gigantea, Sphaerulina giliae, Sphaerulinahainensis, Sphaerulina halophila, Sphaerulina hamadryadum, Sphaerulinahederae, Sphaerulina helicicola, Sphaerulina hyperici, Sphaerulinainaequalis, Sphaerulina inquinans, Sphaerulina intermedia, Sphaerulinaintermixta, Sphaerulina ipomoeae, Sphaerulina islandica, Sphaerulinaiwatensis, Sphaerulina juglandis, Sphaerulina leightonii, Sphaerulinalepidiotae, Sphaerulina limnanthemi, Sphaerulina lini, Sphaerulinalinicola, Sphaerulina ludwigiae, Sphaerulina mappiae, Sphaerulinamarattiae, Sphaerulina marginata, Sphaerulina maroccana, Sphaerulinamarsileae, Sphaerulina maydis, Sphaerulina menispermi, Sphaerulinamicrothyrioides, Sphaerulina mimosae-pigrae, Sphaerulina miyakei,Sphaerulina musae, Sphaerulina muscicola, Sphaerulina muscorum,Sphaerulina musicola, Sphaerulina musiva, Sphaerulina myriadea,Sphaerulina myriadea subsp. myriadea, Sphaerulina myrtillina,Sphaerulina naumovii, Sphaerulina nephromiaria, Sphaerulina oleifolia,Sphaerulina orae-maris, Sphaerulina oryzae, Sphaerulina oryzina,Sphaerulina oxalidis, Sphaerulina oxyacanthae, Sphaerulina pallens,Sphaerulina parvipuncta, Sphaerulina patriniae, Sphaerulina paulistana,Sphaerulina peckii, Sphaerulina pedicellata, Sphaerulina pelargonii,Sphaerulina phalaenopsidis, Sphaerulina phellogena, Sphaerulinaphoenicis, Sphaerulina phyllostachydis, Sphaerulina pini, Sphaerulinaplantaginea, Sphaerulina pleuropogonis, Sphaerulina polygonorum,Sphaerulina polypodii, Sphaerulina polypodii, Sphaerulina polyspora,Sphaerulina populi, Sphaerulina populicola, Sphaerulina porothelia,Sphaerulina potebniae, Sphaerulina potentillae, Sphaerulina poterii,Sphaerulina primulicola, Sphaerulina pruni, Sphaerulinapseudovirgaureae, Sphaerulina pterocarpi, Sphaerulina pulii, Sphaerulinaquercicola, Sphaerulina quercifolia, Sphaerulina quitensis, Sphaerulinarehmiana, Sphaerulina rhabdoclinis, Sphaerulina rhodeae, Sphaerulinarhododendri, Sphaerulina rhododendricola, Sphaerulina rubi, Sphaerulinasaccardiana, Sphaerulina saccardoana, Sphaerulina sacchari, Sphaerulinasalicina, Sphaerulina sambucina, Sphaerulina sasae, Sphaerulinaschaereri, Sphaerulina scirpi, Sphaerulina sepincola, Sphaerulinaserograpta, Sphaerulina silacincola, Sphaerulina smilacincola,Sphaerulina socia, Sphaerulina spartii, Sphaerulina staphyleae,Sphaerulina staurochili, Sphaerulina steganostroma, Sphaerulina subgen.Pharcidiella, Sphaerulina subgen, Sphaerulina, Sphaerulina subglacialis,Sphaerulina subtropica, Sphaerulina suchumica, Sphaerulina tabacinae,Sphaerulina tanaceti, Sphaerulina tarda, Sphaerulina taxi, Sphaerulinataxicola, Sphaerulina thujopsidis, Sphaerulina tiliaris, Sphaerulinatirolensis, Sphaerulina todeae, Sphaerulina trapae-bispinosae,Sphaerulina trifolii, Sphaerulina tritici, Sphaerulina umbilicata,Sphaerulina valerianae, Sphaerulina viciae, Sphaerulina vincae,Sphaerulina violae, Sphaerulina vismiae, Sphaerulina vulpina,Sphaerulina westendorpii, Sphaerulina worsdellii, Sphaerulinaxerophylli, Sphaerulina yerbae, Sphaerulina ziziphi, Sphaerulinazizyphae, and Sphaerulina zizyphi.

Method for Preventing Cell Division of a Human Cell

It has been found in accordance with this disclosure that PANdomain-containing proteins are involved in regulating the rate of celldivision in mammalian cells, and cellular migration in cancer cells.Thus, another aspect of the disclosure is directed to a method forpreventing cell division of a human cell and cellular migration incancer cells comprising inactivating a gene encoding a PAN domaincontaining protein in the human cell.

In some embodiments, the inactivation is achieved by introducing anon-silent mutation in the gene at a residue encoding a conservedcysteine residue of the PAN domain.

In some embodiments, the PAN domain-containing protein is HepatocyteGrowth Factor (HGF), or a homolog thereof. In some embodiments, the HGFbinds to cMET receptor and has an amino acid sequence that is at least70%, 73% 75%, 78%, 80%, 83%, 85%, 88%, 90%, 93%, 95% or 99%, or moreidentical to SEQ ID NO: 49.

In some embodiments, the conserved cysteine residue is selected from aresidue homologous to a cysteine at position 34, 38, 48, or 60 of SEQ IDNO: 32.

In some embodiments, the non-silent mutation is a nonconservativemutation. In some embodiments, the nonconservative mutation is acysteine to alanine mutation.

In some embodiments, the inactivating of the selected gene is achievedby introducing an exogenous nucleic acid inhibitor of the gene encodinga PAN domain-containing protein to the cancer cell.

In some embodiments, the nucleic acid inhibitor is selected from thegroup consisting of an antisense RNA, a small interfering RNA, an RNAi,a microRNA, an artificial microRNA, and a ribozyme.

In some embodiments, the inactivating of the gene encoding a PAN domaincontaining protein is achieved by genome editing, which is achieved by amethod selected from the group consisting of CRISPR/Cas system, Cre/Loxsystem, TALEN system, ZFNs system and homologous recombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the cancer cell a first nucleic acid encoding a Cas9nuclease, and a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the gene.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the cancer cell a first nucleic acid encoding a Cas9nuclease, a second nucleic acid comprising a guide RNA (gRNA), whereinsaid gRNA is specific to the gene encoding a PAN domain containingprotein, and a third nucleic acid comprising a template for homologousrecombination.

In some embodiments, the cancer cell is selected from breast cancer,colon cancer, lung cancer, skin cancer, brain cancer, blood cancer,cervical cancer, liver cancer, prostate carcinoma, pancreas carcinoma,gastric carcinoma, ovarian carcinoma, renal cell carcinoma,mesothelioma, and melanoma.

Methods for Improving In Vitro Fertilization (IVF) Efficiency

It has been found in accordance with this disclosure that sperms andoocytes contain PAN domain-containing proteins that play crucial rolesin the fertilization process. Without being bound by a particulartheory, PAN domain containing proteins are believed to suppress theimmune response by the oocyte, or other cells in the uterus, against thesperm (a foreign entity) and the embryo (partially foreign entity). Somecases of infertility can result from mutations in a PAN domain of a PANdomain containing protein expressed in the reproductive system.

Therefore, another aspect of the disclosure is directed to a method forimproving in vitro fertilization (IVF) efficiency in a non-human subjectsuffering from infertility comprising determining the sequence of a genethat encodes a PAN domain-containing protein, and when a mutation isfound in a conserved cysteine of the PAN domain of the PANdomain-containing protein obtaining an ovum or a sperm from the subject,correcting the mutation in the PAN domain-containing protein in the ovumor the sperm.

In some embodiments, the PAN domain containing protein gene is a ZonaPellicuda(ZP) protein.

In some embodiments, the conserved cysteine residue is selected from aresidue homologous to a cysteine residue in SEQ ID NO: 23.

In some embodiments, the correcting of the PAN domain is achieved bygenome editing by a method selected from the group consisting ofCRISPR/Cas system, Cre/Lox system, TALEN system, ZFNs system andhomologous recombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the ovum or the sperm a first nucleic acid encoding aCas9 nuclease, a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the gene encoding a PAN domaincontaining protein, and a third nucleic acid comprising a template forhomologous recombination that corrects the mutated residue to cysteine.

In some embodiments, wherein the ovum or the sperm are from adomesticated animal. In some embodiments, the domesticated animal isselected from the group consisting of horse, camel, donkey, cat, goat,dog, pig, cow, and sheep.

Methods for Preventing Pregnancy (Immunocontraception)

Another aspect of the disclosure is directed to a method for preventingpregnancy or implantation of a fetus in a non-human subject comprisinginactivating a gene encoding a PAN domain-containing protein in an ovumor a sperm.

In some embodiments, the inactivating is achieved by introducing anon-silent mutation in the gene at a residue encoding a conservedcysteine residue of the PAN domain.

In some embodiments, the PAN domain containing protein gene is a ZonaPellicuda protein.

In some embodiments, the conserved cysteine residue is selected from aresidue homologous to a cysteine a cysteine residue in SEQ ID NO: 23.

In some embodiments, the non-silent mutation is a nonconservativemutation.

In some embodiments, the nonconservative mutation is a cysteine toalanine mutation.

In some embodiments, the inactivating of the selected gene is achievedby introducing an exogenous nucleic acid inhibitor of the selected geneto the ovum or the sperm.

In some embodiments, the nucleic acid inhibitor is selected from thegroup consisting of an antisense RNA, a small interfering RNA, an RNAi,a microRNA, an artificial microRNA, and a ribozyme.

In some embodiments, the inactivating of the selected gene is achievedby genome editing, which is achieved by a method selected from the groupconsisting of CRISPR/Cas system, Cre/Lox system, TALEN system, ZFNssystem and homologous recombination.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the ovum or the sperm a first nucleic acid encoding aCas9 nuclease, a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the selected gene.

In some embodiments, the CRISPR-mediated genome editing comprisesintroducing into the ovum or the sperm a first nucleic acid encoding aCas9 nuclease, a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the selected gene, and a third nucleicacid comprising a template for homologous recombination.

In some embodiments, the ovum or the sperm are from a domesticatedanimal. In some embodiments, the domesticated animal is selected fromthe group consisting of horse, camel, donkey, cat, goat, dog, pig, cow,and sheep.

Methods for Discovering Oncoproteins

As discussed above, PAN domain-containing proteins have been found toplay a role in regulating the rate of cell division. Therefore, anotheraspect of the disclosure is directed to a method for screening for anovel oncoprotein protein in a mammalian cell comprising assessing thesequence of a candidate protein, and determining that the candidateprotein is an oncoprotein when at least one PAN domain is found in thesequence.

In some embodiments, the Plasminogen Apple Nematode (PAN) domain has aconsensus sequence as shown in SEQ ID NO: 23.

In some embodiments, the mammalian cell is an animal cell. In someembodiments, the mammalian cell is a human cell.

Method for Inactivating a PAN Domain Containing Protein

PAN domains are involved in protein-protein interactions (as in HGF andcMET). In addition, it has also been found in accordance with thisdisclosure that introducing a mutation in at least one conservedcysteine of a PAN domain prevents the protein-protein interactions ofthe PAN domain, thereby inactivating the PAN domain-containing proteinand inhibiting its function.

Another aspect of the disclosure is directed to a method forinactivating a PAN domain-containing protein comprising introducing anon-silent mutation in the protein at a conserved cysteine residue ofthe PAN domain.

In some embodiments, the PAN domain-containing protein gene is selectedfrom the proteins listed in List 1.

In some embodiments, the conserved cysteine residue is selected from aresidue equivalent to one of the six cysteine residues in SEQ ID NO: 23.

Unless defined otherwise, all technical and scientific terms used hereinhave the same meaning as commonly understood by one skilled in the artto which this invention belongs. Although any methods and materialssimilar or equivalent to those described herein can also be used in thepractice or testing of the present invention, the preferred methods andmaterials are now described. All publications mentioned herein areincorporated herein by reference to disclose and describe the methodsand/or materials in connection with which the publications are cited.

The specific examples listed below are only illustrative and by no meanslimiting.

EXAMPLES Example 1: Materials and Methods Cloning, Sequencing andOverexpression of G-RLKs

The coding sequences of SapurV1A.0037s0270.1, SapurV1A.0918s0020 andSapurV1A.1175s0020 were amplified by PCR from cDNA derived from Salixpurpurea leaves using HiFi polymerase (Clontech). Sequences weredetermined using Phytozyme using the Salix purpurea v.1.0 genome. ThepENTR/D-TOPO entry vector was used for the insertion of the PCR productsusing the pENTR Directional Topo Cloning Kit (Thermo Fisher Scientific).LR Clonase II Enzyme Mix (Thermo Fisher Scientific) was used to transferthe coding sequences into the pGWB402-omega destination vector andtransformed into One Shot TOP10 Chemically Competent cells. Vectors weretransformed into the Agrobacterium strain GV3101 and transformed intoCol-0 Arabidopsis thaliana using the floral dip method. T1 seeds wereselected with Kanamycin and grown in long day growth chambers at 16/8hours light/dark at 22° C. Three week old leaf tissue was collected forRNA extractions using the Spectrum Plant Total RNA Kit (Sigma) and cDNAsynthesized using the Superscript III Reverse Transcriptase witholigo-d(T) primers (Thermo Fisher Scientific). qRT-PCR was performedusing the PowerUP SYBR Green Master Mix (Thermo Fisher Scientific) andrelative expression for each gene was determined with the 2ΔΔCt methodwith GAPDH as an internal control.

TABLE 1 Primer sequences SEQ ID Primer name Primer sequence NO1_0037s0270csF CACCATGCTTAAGCAGGGCAATTTCT 1 2_0037s0270csRTCATGGTTCCATTGGCCTCT 2 5_0918s0020csF CACCATGGGCGTGACTAGGAATAGAG 36_0918s0020csR CTAAGAGGAGTCTACTTCGACCTC 4 77_RLK53_GWFCACCATGGGTACTTTTTCAGTTCTG 5 78_RLK53_GWRs CTACCGGGCCTCTAATGACATC 623_0037s0270rtF GGGGTCAAAGCTTTCTACAGAGG 7 24_0037s0270rtRGCCAACCAAACCACAGTTTGC 8 27_0918s0020rtF GCTTTTGTGAAGAGGTTGCCATGG 928_0918s0020rtR GACCCCATTTTGAGACACCC 10 89_RLK53_RTF CGTTTCAACCGGAGGAAGC11 90_RLK53_RTR TTACATTCAGAGCCCCCAAAGC 12 177_Arab_WRKY70_RTFCATGGATTCCGAAGATCACA 13 178_Arab_WRKY70_RTR CTGGCCACACCAATGACAA 14179_Arab_WRKY40_RTF AAATCAGCCCTCCCAAGAAACG 15 180_Arab_WRKY40_RTRCTTCACGACAGTCTCTTCTCTCTGC 16 181_Arab_WRKY33_RTF AGGCTCATCGATTGTCAGCA 17182_Arab_WRKY33_RTR CTGCACTACGATTCTCGGCT 18 183_Arab_WRKY8_RTFGTTGTCGGTGATGGTTGTGC 19 184_Arab_WRKY8_RTR CCGGATCTTGCCGGAATCTT 20185_Arab_GAPDH_RTF AGGCCATCAAGGAGGAATCT 21 186_Arab_GAPDH_RTRGAAAATGCTTGACCTGTTGTCAC 22

TABLE 2 Matching primers to genes and use Gene Name Primer name Primeruse SapurV1A.0037s0270 1_0037s0270csF Cloning CDS 2_0037s0270csR CloningCDS SapurV1A.0918s0020 5_0918s0020csF Cloning CDS 6_0918s0020csR CloningCDS SapurV1A.1175s0020 77_RLK53_GWF Cloning CDS 78_RLK53_GWRs CloningCDS SapurV1A.0037s0270 23_0037s0270rtF RT-qPCR 24_0037s0270rtR RT-qPCRSapurV1A.0918s0020 27_0918s0020rtF RT-qPCR 28_0918s0020rtR RT-qPCRSapurV1A.1175s0020 89_RLK53_RTF RT-qPCR 90_RLK53_RTR RT-qPCR WRKY40(AT1G80840) 179_Arab_WRKY40_RTF RT-qPCR 180_Arab_WRKY40_RTR RT-qPCRWRKY33 (AT2G38470) 181_Arab_WRKY33_RTF RT-qPCR 182_Arab_WRKY33_RTRRT-qPCR GAPDH (AT3G26650) 185_Arab_GAPDH_RTF RT-qPCR 186_Arab_GAPDH_RTRRT-qPCRSynteny Analysis Between Oryza sativa and O. punctata

The CDS sequences and corresponding annotation files for O. sativa(IGRSP 1.0) and O. punctata (Oryza_punctata_v1.2) were downloaded fromEnsembl Plants. The CDS files and sequences were then filtered to onlyretain protein coding genes. The protein coding genes were thenannotated with Interproscan 5 (Jones et al., 2014, Bioinformatics, 30.9(2014): 1236-1240). Synteny analysis was then performed via MCScanX andgenes containing a PAN domain were searched against resulting syntenyblocks. Regions that showed evidence of PAN domain expansion wereextracted and visualized with the JCVI utility libraries.

Alignments of G-RLK Sequences

Interproscan 5 was used to identify the PAN domain regions of the 8G-RLKs in FIG. 1. These regions were then extracted and aligned withMAFFT linsi (Katoh et al., Molecular biology and evolution, 30.4 (2013):772-780) and then visualized with Geneious R11.

Domain Prediction in Anopheles gambiae and Diaphorina citri

Interproscan 5 was used to identify domains for the 10 proteins in FIG.2. The proteins were then aligned with MAFFT linsi and aNeighbor-Joining tree was generated with Geneious. The domain structurewas then visualized with GSDS 2.0 (Hu et al., Bioinformatics, 31.8(2014): 1296-1297).

Example 2

A protein database survey revealed that the PAN domain is foundin >28,000 proteins derived from 2,496 organisms representing 959genera. These included organisms with a high propensity to recruitsymbionts, vector parasites and exhibit parasitic or pathogenicbehavior. Additionally, the core conserved cysteine residues of thedomain are structurally similar to cysteine-rich peptides that have beenimplicated in modulation of immune responses. Given the cumulativeobservations, the inventors propose that the PAN domain is a unifyingfeature in immunoregulation (e.g., immunosuppression) across divergentorganism and propose the existence of an ‘immunoregulome’ comprised ofPAN domain proteins functioning to mediate host-cell invasion.

In revealing a novel role for self-immunosuppression in plants duringhost-cell invasion by microbes, the PAN domain proteins, D-mannoselectin kinases (G-LecRKs), were shown to function as negative regulatorsof defense signaling during pathogenesis by the fungal pathogenSphaerulina musiva, parasitism of Arabidopsis by nematodes, andconversion of Arabidopsis into a host of the fungal symbiont Laccariabicolor. Moreover, PAN domain carrying S-locus kinases, reported tomediate self-incompatibility during pollination, fall under the sameclass of G-LecRKs.

In Salix purpurea, the inventors discovered two G-LecRKs(SapurV1A.0037s0270.1 (RLK5) and SapurV1A.0918s0020 (RLK7)) that, uponoverexpression in Arabidopsis, triggered defense responses instead offunctioning as immunosuppressors. Domain annotation using the PFAMdatabase did not reveal presence of a PAN domain in both proteins,however, upon further analyses, the inventors observed that these twoG-LecRKs carried a vestigial PAN domain. Specifically, the inventorscompared the PAN domains of the two Salix G-LecRKs with onesdemonstrated to be immunosuppressive, AT1G61380, Potri.T022200.1 andPotri.005G018000.1 and noted that both had mutations on the conservedasparagine (N) and cysteine (C) amino acids at positions 50 and 51 whileSapurV1A.0037s0270 was also missing the cysteine residue at position 1(FIG. 1). With this observation, the inventors hypothesized that the PANdomain was essential for immunosuppression.

To test the hypothesis that the PAN domain is necessary forimmunosuppression, the inventors sought to evaluate the context in whichit is found in other proteins. We scanned protein databases, InterProand UniProt (https://G-LecRK.uniprot.org), and found >28,000 proteinsacross eukaryotes, archaea, bacteria and viruses carrying the PANdomain. After classifying 2,496 organisms representing 959 genera, into13 categories (Alveolata, Archea, Amoebazoa, Bacteria, Cryptophyta,Euglenozoa, Haptophyceae, Opisthokonta, Rhizaria, Rhodophyta,Stramenopilles, Viridplantae, and Viruses), the inventors observed thatthe domain had high fidelity to co-occurring domains and was found inspecific protein families within each category. For example, inbacteria, the PAN domain was almost exclusively found in associationwith the alpha 2-macroglobulin (A2M) or related domains whereas ineuglenozoa, it was found almost exclusively in association with theglycosyl hydrolase protein domain (FIGS. 6A-6K).

To assess the validity of association with immune modulation, theinventors performed a GO-enrichment analysis using the >28,000 protein.This analysis revealed 39 GO-terms that were enriched at p<0.05. Theseincluded terms like cell recognition (p<1E-30), cell communication(p<1E-30), proteolysis (p<1E-30), pollen-pistil interaction (p<1E-30),reproduction (p<1E-30), response to stimulus (p<1E-30) and response tostress (p<1E-30). These processes are consistent with roles inmodulation of immune responses.

Example 3: Role of PAN Domain Proteins in Gamete Fertilization

Since male gametes are essentially foreign invading bodies,immunosuppression is essential during gamete fertilization, failure ofwhich leads to incompatibility and sterility. As the first interface atwhich male gametes are perceived, the Zona Pellucida (ZP) occurs outsidethe female gamete as a layer of glycoproteins that has been reported torelease species-specific chemoattractants to attract sperms to eggs.Within this glycoprotein matrix, PAN domain-carrying ZP proteins, alsoregarded as sperm receptors, are found as transmembrane proteins. ZPproteins have been widely implicated in modulating fertility across awide variety of eukaryotes including mammalian, avian, amphibian, fish,ascidian and molluscan systems. Bertschinger et al. (Bothalia-AfricanBiodiversity & Conservation, 48(2), 1-8 (2018)) reported that ZPproteins have been successfully used in immunocontraceptive approachesto manage populations of close to 90 animal species.

In plants, the PAN domain-harboring S-locus, serine-threonine, kinaseshave been shown to mediate pollen recognition and incompatibility inplants. PAN domain mediates S-locus receptor dimerization in the absenceof a ligand and suggested that dimerization primes the receptor forinteraction with its ligand to enhance the binding affinity. The S-locusreceptor kinase (SRK) protein, located in the epidermal cells of thestigma, binds to its cognate pollen coat localized S-locus cysteine-rich(SCR) protein to initiate a signaling cascade to rejectself-pollination. However, a non-self SCR protein will not be able tobind the SRK receptor and cross-pollination will occur unimpeded. Thisexample shows that there is specificity between SRK-SCR interactionsthat is likely coordinated by the PAN domain as both the SCR and SRKproteins contain cysteine-rich regions capable of forming disulfidebonds.

Example 4: PAN Domain Proteins Implicated in Cell Growth andProliferation

In animal systems, the PAN domain is found in plasminogen, hepatocytegrowth factor (HGF), coagulation factor XI (FXI) and plasma kallikrein(PK), all protein classes implicated in cell growth, proliferation andregulation of immune system responses. Plasminogen and HGF have asimilar domain structure with a N-terminal PAN domain, multiple Kringledomains and a serine protease domain. HGF in complex with the METreceptor activates a signaling cascade that initiates cell mobility,tissue regeneration, and angiogenesis. HGF/MET has been shown to haveboth an immunosuppressive and an immuno-positive role with dysregulationof HGF/MET signaling in tumors leading to invasion and metastasis.

Example 5: Cell Growth and Proliferation Machinery as a Target forHost-Cell Invasion

FXI and PK are members of the contact system and consist of 4 N-terminalPAN domains followed by a serine protease domain. The contact system isa group of proteins that are activated by coagulation factor FXII. Theybind to surfaces to cause blood coagulation and initiate inflammationresponses. The contact system is activated by surface proteins ofspecific pathogens including, Streptococcus pyogenes, Salmonella, andEscherichia coli. Previous research by Krem and Di Cera (Trends inbiochemical sciences, 27(2), 67-74 (2002)), has suggested that the bloodcoagulation system in vertebrates is an evolutionary by-product of theinnate immune system. This is supported by the role of the contactsystem in initiating a signaling cascade that traps microorganisms in ablood clot to stop their invasion. For example, during Streptococcuspyogenes infection, FXII will bind to the surface of the bacteria andactivate FXI and PK to trap the bacteria in a fibrin clot and induce aproinflammatory response to clear the infection. Activation of thecontact system may also be beneficial to the microbe because the releaseof bradykinin, a product of contact activation system, will increasevascular permeability and provide a nutrient-rich environment for thebacteria to thrive.

Pathogens have evolved mechanisms to evade this host defense response bytargeting another PAN domain-containing protein, plasminogen. Inresponse to the formation of the fibrin clot, S. pyogenes secretesstreptokinase, a protein that converts plasminogen to its active form ofplasmin. Plasmin will degrade the fibrin clot, which allows the bacteriato escape and the infection to spread. S. pyogenes is one of multipleorganisms that target plasminogen to evade the host defense responses.Additionally, parasitic organisms like plasmodium use surface enolase tobind the kringle domain of plasminogen and release plasmin to degradethe extracellular matrix of surrounding tissues and spread theinfection.

Example 6: PAN Domain Proteins Involved in Host-Cell Invasion byParasites

Apicomplexan parasites including, Plasmodium spp., Toxoplasma gondii,Eimeria spp., and Cryptosporidium spp. secrete micronemal proteins thatcontain the PAN domain. Apical membrane antigen 1 (AMA1), is amicronemal protein with orthologs in Plasmodium, the causal agent ofmalaria in humans, Toxoplasma spp., obligate parasites with among thebroadest host range in animals, and Eimeria spp., which infects poultryand cattle. Numerous studies have demonstrated that AMA1 is essentialfor erythrocyte invasion where it has been implicated as a key member ofthe moving junction (MJ) complex. The MJ complex forms at the contactpoint between the parasite and the host cell where inward invaginationof the erythrocyte membrane occurs. Interaction between AMA1 and rhoptryneck protein 2 were shown to be essential for MJ formation. AMA1 hasbeen widely targeted for development of vaccines against multipleparasites and anti-AMA1 antibodies were shown to have efficacy inreducing invasion of the host cell by these parasites. In T. gondii,Gong et al. (2012) reported that the PAN domain-containing protein(P104), which carries multiple PAN domains was necessary for optimalinvasion efficiency. Similarly, genomes of parasitic worms includingTrichinella spp., Ancylostoma spp., Pristionchus spp., which infecthumans, carry numerous PAN domain proteins including antiplateletproteins utilized by Leeches (Haementeria officinalis) to inhibit bloodcoagulation.

Example 7: PAN Domain Protein Among Insect Vectors of Pathogen andParasites

Insect vectors of pathogens and parasites pose major diseaseepidemiological challenges. As such, management of their populationusing chemicals and, more recently, gene-drives to diminish theirpopulations has been a major focus in efforts to contain transmission ofdiseases. Given their global economic importance, the inventors comparedPAN domain proteins from Diaphorina citri, a psyllid vectoring thebacterium Candidatus liberibacter which causes citrus greening andAnopheles gambiae, a vector of the malaria parasite, plasmodium.Consistent with the inventors' hypothesis and despite major differencesin their biology, PAN domains in both organism were found in associationwith the same ZP domain implicated in immunosuppression during gametefertilization above (FIG. 2). The inventors propose that these proteinscould be targeted by parasites during infection to suppress immuneresponses, thus enabling persistence of the parasite inside the insectbody. This proposition offers the opportunity to target these proteinsto lower vector capacity of insects and thus reduce diseasetransmission.

Example 8: Prevalence of PAN Domain Proteins in Infectious Viruses andPathogens

In viruses, long recognized as minimal infectious units, the PAN domainis found in envelope proteins that mostly contain no other recognizabledomains except its close relative, the APPLE domain (FIG. 7). This mightsuggest that, the PAN domain by itself is sufficient forimmunosuppression. However, we also found that in Mimiviruses, whichinclude, the African swine virus, Emiliania huxleyi virus and Niemeyervirus, the PAN domain is found in association with HGF, TMhelix,transmembrane, non-cytoplasmic and a cytoplasmic domain and signalpeptide domains. Mimiviruses, known as giant virus, are recognized fortheir significantly larger genomes that encode proteins with functionsnot typically found in common viruses. Consistent with other complexparasites described above, it appears that Mimiviruses requireadditional manipulation of the host post-immunosuppression to persist intheir host cells.

Among fungi, proteins from Ascomycetes represent 97% of PAN domainproteins reported found in our survey. This class of fungi is wellrecognized for pathogenesis in animals and plants. For example, Fusariumspp. are generally considered harmless, but a subset of these fungi arepotent pathogens causing severe diseases in both plants and humans. Itis noteworthy that based on our survey, five pathogenic Fusarium speciescomplexes carried disproportionately higher numbers of proteins with thePAN domain compared to other netriaceaes (List 1). In order ofdescending-predicted number of PAN domain proteins, these were F.oxysporum, F. fujikuroi, F. sambucinum, F. solani, and Fusariumincarnatum-equiseti. Galactose oxidase, carbohydrate binding andglutathione S-transferase contributed the largest proportion ofco-occurring domains (FIG. 3).

Among heterokonts, proteins of oomycete origin represented 96% of allPAN domain proteins identified in our survey. Aphanomyces astaci, thecausal agent for crayfish plague and Phytophthora spp., one of the mostdamaging plant pathogens and the causal agent of the sudden oak deathepidemic, had disproportionately higher numbers of predicted PAN domainproteins (List 1). Interestingly, the glucose-methanol-cholineoxidoreductase (GMC) domain co-occurs with the PAN domain in bothorganisms. This domain has been implicated in asexual development inAspergillus nidulans, chemical defenses in leaf beetles and cellextension and expansion during metamorphosis in crustaceans. Theinvolvement of these PAN domain proteins in reproduction and cellproliferation is reminiscent of other eukaryotic systems describedabove. Moreover, GMC family proteins are recognized for their role insequestration of the plant host-defense metabolite salicin and henceadaptation of beetle larvae to specific host plants. It is noteworthythat infection of oaks by P. ramorum is often followed by heavyinfestation by beetles, although the exact cause has not beenidentified. Here, the inventors propose that the sequestration of oakdefense-related secondary metabolite by the PAN harboring GMC familyproteins in P. ramorum could mediate the observed attraction of beetlesto infected trees. Similarly, functions performed by GMC proteins in A.astaci could mimic metamorphosis-mediated immunosuppression tofacilitate infection leading to crayfish plague.

Example 9: PAN Domain Penetrance Among Bacterial Symbionts

Assessment of domain presents in the bacteria kingdom revealed that thePAN domain is found predominantly among alpha proteobacteria, wellrecognized for their host-cell invasion and symbiosis behavior. Of the1,783 bacterial proteins carrying the domain, 1,587 (89%) were found inRhizobium sp. and Rhodobacter sp. (List 1). These bacteria arespecialized in nodulation of land plants and symbiosis with marinedanoflagellates, respectively. The PAN domain was almost exclusivelyfound in anti-peptidase proteins and co-occurred with the A2M domain orrelated macroglobulin domains (FIG. 2). A2M is recognized as abroad-spectrum protease inhibitor that has been widely implicated inimmune modulation and is associated with a wide array of diseases. Asidefrom its anti-protease activity, A2M has binding affinity to a widevariety of molecules. In both Rhizobium sp. and Rhodobacter sp., hemesequestration is an essential process for the survival of bacteriainside host cells. The exact mechanism underlying this process hasremained largely elusive with limited progress in identifying proteinsrelated in to heme sequestration. Here, the inventors note that A2M hasbeen previously reported to function as a Hx:heme receptor, known as theLow-density lipoprotein receptor-related protein-1 (LRP1). LRP1 wasshown to play a central role in heme scavenging after intracerebralhemorrhaging in mice. With this observation, the inventors propose thatthe PAN domain may have been co-opted to act as an immunosuppressantwhile the A2M domains functions to sequester heme and create thenecessary environment for bacterial survival in plant host cells.

Example 10: Domain Expansion in Organisms Specialized in SymbiontRecruitment

Numerous organisms such as corals, planktonic crustaceans and plantsdepend on symbionts to perform essential functions. In these instances,immunosuppression is a key step in conferring compatibility betweenhosts and symbionts. For example, Daphnia magna is a planktoniccrustacean that is considered a model system to study host-parasiteinteraction since it has highly diverse internal microbiome. Evaluationof PAN domain genes in its genome revealed occurrence of duplicated genein the protein families such as Brain chitinase, Chorion peroxidase,Class A scavenger receptor (cA-SR) with a serine protease domain,Coagulation factor XI, No mechanoreceptor potential (nomp) A-like,Peroxinectin (PX)-like, putative Transmembrane protease serine, ZP aswell as multiple uncharacterized protein. The participation ofChitinase, Coagulation factor XI, proteases and ZP protein inimmunosuppression-related proteins was discussed above and cA-SRs havebeen studied for their function in innate immunity. Akin to D. magna,plants also recruit symbionts to perform essential functions includingnutrient mobilization. The inventors note that G-LecRKs implicated inimmunosuppression during recruitment of fungal symbiont above occur as alarge protein family with hundreds of members and exhibit frequentgene-expansion across plant genomes (FIG. 5). The inventors hypothesizethat both these organisms coopted immunosuppressive proteins tofacilitate their symbiotic lifestyle by allowing rapid expansion ofthese genes within their genomes.

Example 11: PAN Domain Similarity to Cysteine-Rich AntimicrobialPeptides

Cysteine-rich peptides (CRPs) are produced by multicellular organismsand are known for their use as antimicrobials. While these peptides arenot considered PAN domain-containing peptides, they have functional andstructural similarities to the PAN domain in that they consist ofconserved cysteine residues that form disulfide bonds and are involvedin immune modulation. The CRP protein, TAP, was first isolated frombovine tracheal mucosa and were noted to have antimicrobial properties.Defensins are a class of CRPs common to both plants and animals and areinvolved in host innate immunity. CRPs are secreted by plants and havebeen shown to be involved in plant defense, symbiotic relationships withbacteria, development, reproduction and pollen-tube guidance. Thenodule-specific cysteine-rich (NCR) peptides are a subclass of CRPs inplants that are secreted by the host plant and regulate symbiosisbetween legumes and rhizobia during nodule development and nitrogenfixation. The structure of NCRs resembles plant defensins that areinvolved in regulating plant innate immunity, but they have a differentfunction in that they regulate symbiosis with rhizobia during nitrogenfixation. Given their structural similarity, it is plausible that CRPsfunction as ligands targeting PAN domain proteins to modulateimmunosuppression.

Example 12: Functional Role of the HGF PAN Domain in Human Cell Lines

c-MET is a receptor tyrosine kinase which is present on the surface ofvarious epithelial cells. c-MET gets activated by binding with itsligand, HGF. HGF is an important paracrine mediator of growth, invasionand angiogenesis in several cancers. All biological impacts of HGF aretriggered by stimulating its cell surface receptor, c-MET with relatedactivation of downstream effector pathway. Upon binding with its ligand,HGF ligand bound c-MET receptor gets internalized via endosomalinternalization and undergo lysosomal degradation. HGF possesses acanonical 4 conserved cysteine residues in its PAN domain whose functionremains to be determined (FIG. 8).

Example 13: Mutating Cysteine Residues in PAN Domain Results in EnhancedHGF Stability

To determine the function of the cysteine residues on the PAN domain,wild type HGF was subjected to mutagenesis and four conserved cysteine(C) residues on PAN domain were mutated to alanine (A) and one conservedasparagine (N) was mutated to aspartic acid (D). HEK293T cells weretransfected with Flag tagged wild type and Flag tagged PAN mutants HGFwhich are HGF 4Cys-4Ala and HGF N-D. Lysates were resolved on a SDSpolyacrylamide gel, transferred to PVDF membrane and probed sequentiallywith antibodies for Flag tagged HGF and endogenous Actin.

Lane 2 of FIG. 9 shows that HGF with four cysteine mutations in PANdomain (HGF 4Cys-4A) had higher stability compared to wild type HGF(Lane 1) when probed against HGF-Flag (FIG. 9). Actin was shown as aloading control. This data suggests that cysteine residues on the PANdomain of HGF mediate proteolysis of the HGF protein.

Example 14: Activation of MET Signaling is Attenuated by the CysteineResidues Mutations in HGF PAN Domain

Once activated, the HGF/c-MET undergoes a rapid internalization fromcell membrane to cytoplasm for degradation/recycling depending on thecellular demand. To address whether the PAN mutant HGF displays morestability as a result of MET binding capability, the inventors studiedthe endogenous c-MET expression in HEK 293T cells overexpressed withwild type HGF and PAN mutants HGF. FIG. 10 topmost panel shows 4Cys-4AlaHGF was unable to activate HGF-c-MET signaling pathway as evident bystable MET expression. The enhanced stability of the MET receptorindicates that the receptor is retained on the cell surface.

Both wild type HGF and N-D HGF could bind c-MET and activates thecascade results in MET degradation. Signaling downstream from METreceptor is mediated through the recruitment of other adaptor proteinsincluding STAT3 and AKT which are stably expressed in cells even aftersignaling cascade activation. In FIG. 10, both middle and lower panelshowed the presence of both STAT3 and AKT in cells under allcircumstances demonstrating the specificity of the HGF PAN for c-MET.This data for the first time, demonstrates a direct link betweenCysteine rich PAN domain with HGF function and c-MET signaling.

HEK 293T cells were transfected with Flag tagged wild type HGF and Flagtagged PAN mutants HGF which are HGF 4Cys-4Ala and HGF N-D. Lysates wereresolved on SDS-polyacrylamide gel, transferred to PVDF membrane andprobed sequentially with antibodies for c-MET, AKT, STAT3 and Actin.FIG. 10, lane 2 in top panel shows significantly higher c-MET stabilitycompared to lane 1 with overexpressed wild type HGF. Lane 4 withoverexpressed empty plasmid showed same c-MET stability as lane 2. Thisconfirms HGF 4Cys-4Ala cannot turn on the c-MET signaling and therebyc-MET is not getting degraded. Immunoblot against AKT and STAT3 showedthe degradation is c-MET specific as both proteins were stable under allconditions. Actin was used as a loading control.

c-MET is a heterodimer consisting of an extracellular α-chain and atransmembrane β-chain connected through a disulfide bridge. Activationof the MET receptor through HGF binding promotes the autophosphorylationon the tyrosine residues on the intracellular domain of c-MET. Thisopens a docking site for the recruitment of other signaling proteinultimately establish a downstream signaling cascade and biologicalresponse. HGF-cMET signaling cascade triggers the activation ofphosphatidylinositol 3-kinase (PI3K) and AKT pathway well defined incell migration. Besides that, the mitogen activated protein kinase(MAPK) and the extracellular kinases (ERK1/2) are well known downstreammediator of this MET signaling cascade. Abnormal activation of c-MET-HGFcascade has been reported to promote the progress of multiple cancersincluding glioblastoma, liver, lung, breast, colon to name a few. In allthose cancers, activated PI3K/AKT, JAK/STAT and Ras/MAPK pathways havebeen reported to be elevated. All these have negative impacts on thecancer prognosis.

To evaluate the effect of PAN mutations on HGF at a biochemical level,the inventors performed western blotting on the protein lysates derivedfrom HEK293T cells stimulated with wild type HGF and 4Cys-4Ala HGF PANmutant proteins for the indicated time (FIG. 19). FIG. 19 topmost panelshows, 4Cys-4Ala HGF PAN mutant was unable to activate c-MET as evidentby the lack of phosphorylation compared to the wild type (WT) HGF.

However, activation of MET receptor with WT HGF results with WT HGFresults the downstream activation of MET signaling cascade as pAKT andpERK levels increased (FIG. 19, panel third and fifth) over time.Mutations on Cysteine residues on PAN were able to completely block theAKT and MAPK pathways.

HEK 293T cells were grown on 6 cm plates and stimulated with both WT HGFand 4Cys-4Ala HGF proteins for the indicated amount of time. Lysateswere resolved on SDS-polyacrylamide gel, transferred to PVDF membraneand probed sequentially with antibodies for pMET, c-MET, pAKT, AKT,pERK, ERK and Actin.

The proto-oncogenic receptor tyrosine kinase c-MET and HGF reported tobe deregulated and promote malignancy in cancer and brain tumors. Theinventors investigated the impact of PAN mutations on cMET activation inglioblastoma cell lines U87. Human glioblastoma cell line was used andwestern blotting on cell lysate were performed following the WT and4Cys-4Ala HGF stimulations for the indicated amount of time (FIG. 20).The results show that PAN mutations on HGF had similar negative impacton cMET signaling cascade activation in glioblastoma cell line.

Analysis of HGF PAN Mutations on cMET Activity in Cells. Mutations inHGF PAN Domain Alters the Localization of cMET in Cells.

It has been well described before that upon HGF stimulation, cMET getsactivated by tyrosine autophosphorylation and is rapidly internalizedand translocate to the nucleus. Following the stimulation, c-MET israpidly internalized to early endosomes and translocate to the nucleuseither to initiate calcium signals and or to upregulate PAX5, atranscription factor, in the nuclear compartment. Here we demonstratethat 4Cys-4Ala PAN mutant HGF failed to activate the cMET translocationto nucleus as compared to the WT HGF stimulation. HeLa cells were grownon 24 well plates before stimulated with both WT and 4Cys-4Ala PANmutant HGF proteins for 30 minutes where indicated. Cells were thenfixed, permeabilized and observed against cMET using fluorescencemicroscope. The fluorescence images confirmed that cMET redistributes tothe region of nucleus from cell membrane following WT HGF stimulationbut not by the 4Cys-4Ala PAN mutant HGF.

PAN Domain Positively Impacts on Cell Proliferation.

To investigate the role of HGF on cell cycle, HGF WT and 4Cys-4Ala PANmutant HGF were used as an exogenous factor to determine its impact oncell proliferation. HEK 293T cells were grown in 96 well plates andstimulated with 100 ng/mL WT HGF and 4Cys-4Ala PAN mutant HGF for 0, 24and 48 hr. MTT, (3-(4,5 dimethylthiazol-2-yl)-2,5-diphenyltetrazoliumbromide) reagents were added and absorbance were measured according tomanufacturer instructions. There was a significant drop in theabsorbance of the cells treated with PAN mutant HGF compared to WT HGFstimulated one (FIG. 21). The absorbance is related to cellproliferation. This observation confirmed a direct evidence ofattenuation of cell proliferation over HGF PAN mutations. This alsoconfirmed that targeting four cysteine residues on the PAN domain of HGFcan attenuate the cell proliferation which is otherwise elevated indifferent cancers.

Investigation of Transcriptional Profiles Upon the Stimulation of Cellswith PAN Mutant HGF.

HGF has been demonstrated to stimulate cancer proliferation, migrationand metastasis by increasing the migration and expression of matrixmetalloproteinases (MMPs) in human. To further address the impacts ofPAN mutations on HGF towards cell, the inventors quantified relativemRNA level of cMET, MMP9, and β-actin by real time-PCR according to theprotocol following stimulation with WT HGF and PAN mutant HGF. FIGS.22A-22B show that interaction between HGF-cMET is important for theupregulation of cMET and MMP9 in HEK 293T cells.

Glioblastoma is the most severe brain tumor type with the highestmalignancy and lowest prognosis. MMPs can enhance the invasive abilityof tumor cells by degrading extracellular matrix proteins (such ascollagen, fibronectin and proteoglycan) as well as growth factor bindingprotein, growth factor precursor, receptor tyrosine kinase, celladhesion molecule and other proteases. Among the MMPs, the elevatedexpression level of MMP2 is meticulously related to the progression ofglioblastoma malignancy. The inventors further explored the relativemRNA level of MMP9 and MMP2 along with c-MET in glioma cells followingHGF stimulation (FIGS. 22C-22E). U87 cells were stimulated with WT HGFand 4Cys-4Ala PAN mutant HGF for 18 hr. Cells were collected and RNAexpression level were determined. FIGS. 22D-22E show the relativeabundance of MMP9 and MMP2 were low upon PAN mutant HGF treatment ascompared to WT HGF stimulation.

Example 15: RLK PAN Domain Mediates G-lecRLK Dimerization

The PAN domain possesses the characteristic 6-cysteine residues in itscore that are highly conserved. These cysteine residues coordinate threedisulfide bridges to form a hairpin structure. The inventorshypothesized that cysteine rich PAN domain of G-lecRLKs form disulfidebonds involved in dimerization and subsequent receptor proteolysis toprevent downstream signaling cascades. To address this hypothesis, a GFPtagged PAN domain construct of RLK5 was made. In addition, mutated aminoacids in the RLK5 vestigial domain were restored to consensus PAN domainamino acids based on the alignment in FIG. 1, this construct wasdesignated RLK5-restored (RLK5R). Both RLK5 and RLK5R constructs weretransfected and overexpressed in HEK293 cells. Proteins were purified onGFP column and loaded into size exclusion column (SEC) to analyze theoligomeric state. Consistent with the inventors' hypothesis, thisbiochemical assay showed that RLK5R could form dimer in SEC whereas RLK5could not (FIGS. 12A-12B).

Example 16: RLK PAN Domain Enhances Receptor Degradation Via MAP KinasePathway

Pattern recognition receptors recognize invasive microbe-associatedsignals and confer host immunity by triggering the initial layer ofplant defense to prevent pathogen proliferation. Previous studies haveshown the importance of MAP kinase (MAPK) in plant innate immunity. ThisMAPK cascade consists of the MAP kinase kinase kinase, YODA, MAP kinasekinases MKK4 and MKK5, and MAP kinases MPK3 and MPK6. MAP kinasesundergo phosphorylation mediated activation. In Arabidopsis, prolongedactivation of MPK3 and MPK6, two kinases critical for pathogenresistance, results in the inhibition of photosynthesis and accumulationof reactive oxygen species (ROS) in chloroplasts.

The inventors wanted to test whether PAN domain containing G-lecRLKsundergo dimerization which prevents the phosphorylation mediatedactivation of downstream signaling cascade. To inventors first performedCycloheximide (CHX) stability assay. Both RLK7 (PAN mutated variant fromSalix described above) and RLK7R (PAN domain restored to consensus aminoacid sequence) were overexpressed in Arabidopsis protoplast followed byCHX treatment at indicated time points, to inhibit the protein turnover. Lysates were resolved with SDS-PAGE gel and documented withchemiluminescence BIO-RAD gel doc system. Resulting data indicated ahigher half-life or extended stability for RLK7 over RLK7R following 0-4hr time points (FIG. 13A). Consistent with expected downstreamphosphorylated of MAP kinases, the inventors observed an overallincrease in the MPK3 and MPK6 phosphorylation (FIG. 13B).

Since the apparent protein instability of RLK7R resulted in itsinability to trigger phosphorylation of MPK3 and 6 as well as subsequentdefense response, the inventors hypothesized that RLK5 and RLK7 withmutated PAN domains lost their immunosuppressive roles and thus shouldtrigger defense signaling.

Example 17: Central Player of Innate Immune Cascade, MAPKs are Activatedin RLK5 and 7 Overexpressed Transgenic Lines

Mitogen activated protein kinases (MAPKs) are well conserved proteinkinases in eukaryotes where MAPK kinase kinase (MAPKKK) activates MAPKkinase (MAPKK) which ultimately activates MAPKs. Upon the detection ofany external stimulus or environmental changes at the cell surface,MAPKs gets upregulated and participates in the classical signaltransduction of immune responsive genes. After overexpression of RLK5and RLK7 in Arabidopsis, the inventors were interested to evaluatewhether any signature MAPKKK and MAPK were activated. Upstreamregulators of this pathway like MAPKKK13 and MAPKKK14 were highlyupregulated in transgenic lines (FIGS. 14A-14B). Additionally, theinventors were interested in studying the regulation of downstreamMAPKs. MAPK3 is one of the most well-known signature gene of thispathway and showed a significant upregulation in transgenic linessuggesting RLKs with mutated PAN domains could induce immune signalingvia MAPK pathway in plants (FIG. 14C).

Example 18: RLK PAN Activates Proteins Involved in JA/ET Pathway

The expression level of the genes related to Jasmonic acid (JA)synthesis were also examined. As shown in FIG. 15B, the inventors wereinterested to observe the signature genes of the JA and ethylene signaltransduction (ET) pathway. LOX3, LOX4 and JAZ5 are the signature genesof JA pathway and are upregulated in transgenic lines compared to wildtype. Other signature genes involved in ET and JA pathways are ERF13,ACS11 and ACS7. These mediators are also upregulated in our transgeniclines. This data suggests that constitutive overexpression of RLK5 andRLK7 in Arabidopsis activates JA and ET pathway (FIGS. 15A-15F).

Example 19: RLK PAN Attenuates Salicylic Acid Pathway of Plant InnateImmunity

Salicylic acid (SA) is an important signal molecule in plant defenseresponse. One essential player in the SA defense response pathway isnon-expresser of pathogen related genes 1 (NPR1). NPR1 is a positiveregulator of SA pathway. It is well known that Arabidopsis npr1 mutantshows increased disease susceptibility and downregulation of genesspecifically pathogen related (PR1) gene. PR1 genes were downregulatedin transgenic Arabidopsis constitutively expressing RLK5 and RLK7 (FIG.16A). In contrast, NPR3 was significantly overexpressed in transgeniclines compared to wild type (FIG. 16B). From these results, theinventors conclude that constitutive expression of RLK5 and RLK7contributed to the regulation of SA related genes and appeared tosuppress the activation of SA signaling pathway.

Example 20: Classical WRKY Genes are Hyperactivated in RLK PANTransgenic Plants

WRKYs are transcription factors involved in various plant processes butnotably in fighting against diverse biotic and abiotic stresses. WRKY18,WRKY33 and WRKY40 are the prominent WRKY genes involved in plantimmunity and the inventors determined significant upregulation of thesetranscription factors in transgenic lines as shown in FIGS. 17A-17C.

A proposed model for function of the PAN domain in plant G-lecRLKs isfound in FIG. 18.

List 1: List of UniProt IDs for PAN Domain Containing Proteins AcrossSpecies.

R4G2C1, R4G7D0, G8EBH2, G8EBN0, G8EDK5, A0A3T1CXD4, A0A3T1CXP1,A0A1E1EXB1, A0A1E1ETK2, A0A1E1EUC2, L8GVM1, L8GRF2, L8GX08, L8GY48,L8H5C9, L8GYA1, J3E810, J2YWZ6, J3IYU5, A0A2L2DLV0, A0A2L2DIZ7,A0A0G2Y717, E3VZX8, E3VYF9, F8V6R0, A0A0G2Y378, A0A0G2Y8U4, A0A2L2DJ09,Q5UPR5, Q5UNW8, Q5UQG0, A0A2L2DM38, A0A0G2Y3S5, A0A0G2YB83, A0A0G2Y7I9,L7RC65, L7RC22, L7RCU4, A0A091MSS1, A0A091MQE1, A0A3Q1FYN5, A0A3Q1FW77,A0A3Q1EDF5, A0A3Q1G8B6, A0A3Q1F1Z0, A0A3Q1I407, A0A316YDH8, A8ZR36,A0A0A7CPG5, A0A0A7CP60, A0A0A7CN07, A0A0A7CNR8, A0A0A7CN57, A0A0A7CP35,A0A0A7CMN8, A0A0A7CP65, A0A0A7CP71, A0A0A7CN98, A0A0A7CP31, A0A1V9ZRA5,A0A1V9ZDE5, A0A1V9YLY7, A0A1V9Z1A6, A0A1V9ZKZ6, A0A1V9Z451, A0A0A7CNG8,A0A1V9YJ62, A0A0A7CMR5, A0A0A7CPD7, A0A1V9Z629, A0A0A7CPH5, A0A1V9YJK3,A0A1V9YSE1, A0A1V9YDS4, A0A1V9YHW9, A0A0A7CMJ7, A0A0A7CN31, A0A1V9ZMC6,A0A0A7CNG9, A0A1V9YH26, A0A1V9YUS3, A0A1V9ZRD0, A0A0A7CNY9, A0A0A7CM59,A0A1V9ZKR0, A0A1V9ZUM1, A0A1V9YUE0, A0A1V9YRF9, A0A1V9ZB07, A0A0A7CN88,A0A1V9YXW4, A0A1V9Z9X3, A0A0A7CLM9, A0A1V9Z933, A0A1V9YWJ8, A0A2E4CB18,A0A2E4CBG1, A0A2E4CB13, A0A2E4CBJ3, A0A2V9ZGI7, A0A150V788, A0A150VFP3,A0A3A1WDE8, A0A444V1E0, A0A444V1E2, F4X7R3, F4X293, F4X6U6, F4X815,F4WMQ5, F4X291, A0A058ZM17, A0A037ZPD6, A0A2R6Q4L0, A0A2R6RAZ9,A0A2R6Q6W9, A0A2R6QV86, A0A2R6QWW6, A0A2R6PXQ8, A0A2R6R4I5, A0A2R6PR71,A0A2R6RB30, A0A2R6P2X1, A0A2R6R7U2, A0A2R6QA16, A0A2R6PTF8, A0A2R6Q077,A0A2R6QTI6, A0A2R6R4H6, A0A2R6QBV2, A0A2R6PQK3, A0A2R6QCM9, A0A2R6RF49,A0A2R6QDU5, A0A2R6QLP2, A0A2R6PTF3, A0A2R6PGN0, A0A2R6RRI6, A0A2R6RGA0,A0A2R6PWC1, A0A2R6PXW3, A0A2R6Q3G8, A0A2R6Q7Z3, A0A2R6QBX6, A0A2R6QLN4,A0A2R6PTE6, A0A2R6QWB9, A0A2R6PJ76, A0A2R6RP34, A0A2R6RB22, A0A2R6QXS9,A0A2R6PEE6, A0A2R6NZR5, A0A2R6RB09, A0A2R6PQU7, A0A2R6QLP8, A0A2R6QC53,A0A2R6PUZ3, A0A2R6PTE5, A0A2R6QBV5, A0A2R6RB02, A0A2R6QCD9, A0A2R6QBW7,A0A2R6R4H9, A0A2R6QWW7, A0A2R6PK86, A0A2R6NKZ3, A0A2R6PRE4, A0A2R6PY69,A0A2R6RB03, A0A2R6QDU9, A0A2R6P887, A0A2R6QXB5, A0A2R6QA21, A0A2R6PRM8,A0A2R6QMJ8, X1WJB0, J9K2R9, J9LS79, J9KAI5, J9KPT6, J9JPB7, J9K0U0,J9JMX3, B3G4G6, B3G448, B3G4F0, A0A1S4G3R5, Q1HRG8, A0A1S4FK22, Q16Y69,A0A1S4FG50, Q16VE9, Q17JC8, Q171P7, Q17FY1, Q16VE8, A0A182H4K1,A0A182H5Q1, A0A182G6M4, A0A182G9D3, A0A182G9D4, A0A452XH92, A0A452ZGN2,A0A453BYP1, A0A453LJQ2, A0A452ZGI7, A0A453HQH7, A0A453AAT9, A0A453DBA5,A0A453BBE0, A0A453BYQ0, A0A453LK80, A0A453ADR6, A0A453Q2G0, A0A452Z039,A0A452ZI33, A0A453D3G9, A0A453DYZ0, A0A453JHI0, A0A453Q2D1, A0A453LKE2,A0A453F7F0, A0A453GM45, A0A452Y396, A0A453BYT2, A0A453MEH1, A0A453EGG7,A0A453D372, A0A453SRN1, A0A453FPM7, A0A453BYQ9, A0A453ADP5, A0A453JI06,A0A453DD86, A0A453LKD6, A0A453DYQ0, A0A453ADU5, A0A452XJR0, A0A453JGU6,A0A453NKE5, A0A453LKC6, A0A453D3I3, A0A453JIH7, A0A453LKE3, A0A453DBY7,A0A453SVX0, A0A453FPN7, A0A453DDB2, A0A453DB66, A0A453FPT3, A0A453DAW9,A0A452XJW5, A0A453DYR4, A0A453LKH1, A0A453DBP7, A0A453NKT3, A0A453ADR2,A0A453D3G3, A0A453AAM1, A0A453D3A4, A0A453PQK2, A0A453Q1Y2, A0A453LKA1,A0A453MGE8, A0A453F7I6, A0A453FPR4, A0A453D383, A0A452Z010, A0A453QTP8,A0A453FPN3, A0A453JHT4, A0A453FPT0, A0A453FPK6, A0A453EGB1, A0A453QZE9,A0A453BYN4, A0A453KBQ0, A0A452Z4D8, A0A452ZEX2, A0A453SHI0, A0A453D306,A0A453FPP1, A0A453F7D3, A0A453LN14, A0A453LK85, A0A453LK71, A0A453H3Z1,A0A453DYX5, A0A453FPQ5, A0A453DBC1, A0A452ZGJ2, A0A452ZGK8, A0A452ZEZ6,A0A453LK88, A0A452YZZ8, A0A453D3A8, A0A453LKC7, A0A453GLW6, A0A453LK95,A0A453LK89, A0A453D358, A0A453QZ76, A0A453GMC5, A0A453BYQ7, A0A453T0W6,A0A453DD79, A0A453BBQ0, A0A453Q244, A0A453DBN0, A0A453GM60, A0A453D325,A0A453Q771, A0A453BCU3, A0A452XK72, A0A453DBI2, A0A453QZN5, A0A453HAH1,A0A453FPI6, A0A452Z002, A0A453LKB1, A0A452XK48, A0A453BBD4, A0A453Q2E7,A0A453QZF2, A0A453DBB2, A0A453JEW1, A0A453SU32, A0A453FPN4, A0A453DBG7,A0A453D337, A0A453LKF9, A0A453F7G5, A0A453SVW0, A0A453BC35, A0A453D3B0,A0A453DA54, A0A453TAB1, A0A453D3G4, A0A453JHJ1, A0A453SRL9, A0A453ADQ2,A0A453D349, A0A453PFF2, A0A453DA76, A0A452XH56, A0A453DC09, A0A453QTY7,A0A453DB70, A0A453DBM7, A0A453FPK2, A0A453DBH5, A0A453Q2F9, A0A453ADR3,A0A453DDD0, A0A452Z027, A0A453FPS3, A0A453D6J6, A0A453J9S0, A0A453Q2M7,A0A453LJR3, A0A453D329, A0A453GM00, A0A453BYP5, A0A453BBD9, A0A453BYM4,A0A453Q291, A0A453QU71, A0A453H3Z4, A0A453SGZ7, A0A453ADQ4, A0A453LKC4,A0A453LKG3, A0A453DBI3, A0A453DC06, A0A453SRP6, A0A453SRK1, A0A453ADR9,A0A453QZE3, A0A453D3H5, A0A452Z019, A0A452Y3L8, A0A453DB32, A0A453D353,A0A453H9U8, A0A453DBK3, A0A453DBC7, A0A453NLT6, A0A453ILU0, A0A452ZQ21,A0A453DBV6, A0A452Z009, A0A453DDA0, A0A453G5Z3, A0A452ZGN5, A0A453D6L7,A0A453BYQ2, A0A453D2Z9, A0A453DBL2, A0A453DBD7, A0A453FPV1, A0A453D352,A0A453Q591, A0A452ZI59, A0A453Q2L2, A0A453D333, A0A453TA51, A0A453DDL7,A0A453G617, A0A453D2X4, A0A452XD19, A0A453Q1X4, A0A453MGQ3, A0A453HRF8,A0A453EGH4, A0A453HQJ5, A0A453LN67, A0A453DB22, A0A453BDB4, A0A453LK93,A0A453DDM1, A0A453D369, A0A453DBK6, A0A453SRN7, A0A452ZGM5, A0A453D6Q2,A0A453LKB4, A0A453BYR3, A0A453D3C0, A0A452XD37, A0A453DDM6, A0A453ADV9,A0A453FPM3, A0A453TAE6, A0A453BC47, A0A452XK40, A0A453F7D6, A0A453NKD5,A0A453DC51, A0A453DBE4, A0A453T114, A0A453BYS4, A0A453H3Z7, A0A453ATP0,A0A453G6T0, A0A452XZ51, A0A453DBW3, A0A452XD28, A0A453LJR8, A0A453BB79,A0A453D382, A0A453LK83, A0A452ZI63, A0A452XZD5, A0A452Z4E2, A0A453T139,A0A453DB02, A0A453FPR7, A0A453PFD9, A0A453BBJ6, A0A453LK79, A0A453BBV1,A0A453DBL5, A0A453FPR9, A0A453D361, A0A452XD46, A0A453QZU7, A0A453ATS1,A0A453FPJ1, A0A452XB26, A0A453QTW5, A0A453BYP4, A0A453D323, A0A453ADR1,A0A452XJS2, A0A453FPS0, A0A453FPQ0, A0A453JB99, A0A453DBF2, A0A453KC08,A0A452XJG0, A0A453DBT2, A0A453IFX4, A0A452XK35, A0A453D3B3, A0A453LJU7,A0A453JH21, A0A453S9X2, A0A452XJT3, A0A453DBV3, A0A452Z033, A0A452XH89,A0A453SAP2, A0A453BBW1, A0A453DC15, A0A453DBY3, A0A453DDL1, A0A453D3A1,A0A453D396, A0A453H3Z3, A0A453EGJ2, A0A453DBW8, A0A453LKB3, A0A453EGJ7,A0A453G694, A0A453Q4I2, A0A453CF81, A0A453FPL3, A0A453GM65, A0A453GMJ9,A0A452Y3H0, A0A453D3A3, A0A453DDC2, A0A452ZNP1, A0A452ZGK3, A0A453DBU3,A0A453GQY1, A0A453IM88, A0A453D363, A0A453SRL5, A0A453Q2A6, A0A453JHH1,A0A453BBU6, A0A453JFZ5, A0A453H3Z2, A0A453DBR3, A0A453DBP2, A0A453LK56,A0A453TAD7, A0A453JH11, A0A453FPS4, A0A452ZGP0, A0A453QZV2, A0A453Q1W1,A0A452XH97, A0A453D2W3, A0A453SVQ7, A0A453DBR6, A0A453EGJ0, A0A453MGF3,A0A453D3B5, A0A453BC42, A0A453Q2K8, A0A453K9H8, A0A453LJN7, A0A453DBK2,A0A453BBR3, A0A453AAL0, A0A453SRP1, A0A453FPQ4, A0A453DBE5, A0A453QU60,A0A453SRQ7, A0A453QUA8, A0A453SUC2, A0A453A3H4, A0A453BYQ1, A0A452XD39,A0A453TAB6, A0A453FPV0, A0A452ZGM7, A0A452ZI86, A0A453SAJ3, A0A453DBS2,A0A453D394, A0A453DB45, A0A452ZGN4, A0A452Z015, A0A452ZNQ3, A0A453BBE7,A0A453LK78, A0A453F7K0, A0A453LKB7, A0A453D375, A0A453DB42, A0A453FPS1,A0A453D385, A0A453LKJ9, A0A453SRH1, A0A453SVF0, A0A453BBF4, A0A453QU28,A0A453SGI2, A0A453DBL7, A0A453AAP4, A0A453KCJ5, A0A453D310, A0A453DC24,A0A453D3E6, A0A453H3Z9, A0A453TA82, A0A453FPU6, A0A453SGY8, A0A453LK90,A0A452ZQ32, A0A453EGC1, A0A453D390, A0A452XB18, A0A453LKE6, A0A452ZRM6,A0A453LKA2, A0A453EGK8, A0A452Z021, A0A453DDC6, 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A0A438HS08, A0A438IT97, A0A0G4H1K6, A0A0G4FPW0,A0A0G4EVW8, A0A0G4G2P6, A0A0G4EX32, A0A0G4EK41, A0A0G4GV94, A0A0G4FK32,A0A0G4FSG0, A0A0G4GBE1, A0A0G4FEA5, A0A0G4G667, A0A0G4G5L3, A0A0G4GUX0,A0A0G4H7X7, A0A0G4FED4, A0A0G4GC70, A0A0G4EL21, A0A0G4EFA5, A0A0G4FS69,A0A0G4G6X5, A0A0G4GSW5, A0A0G4FB70, A0A0G4FJV3, A0A0G4ELW9, A0A0G4F302,A0A0G4H591, A0A0G4GFR4, A0A0G4FNT8, A0A0G4H797, A0A0G4FKH8, A0A0G4GBQ5,A0A0G4G8Z9, A0A0G4FBG5, A0A0G4FUC6, A0A0G4EES0, A0A0G4GY87, A0A0G4FN79,A0A0G4FG97, A0A0G4GU04, A0A0G4GAX4, A0A0G4EKA7, A0A0G4E9C4, A0A0G4GA99,A0A0G4GC21, A0A0G4F4H5, A0A0G4GTL7, A0A0G4EC69, A0A0G4EDQ0, A0A0G4F1H0,A0A0G4GX24, A0A0G4GSZ4, A0A0G4GQI0, A0A0G4FAD2, A0A0G4EYY7, A0A0G4ECR3,A0A0G4FRN1, A0A0G4F3I1, A0A0G4GJ27, A0A0G4FWK0, A0A0G4FT88, A0A0G4ER04,A0A0G4FH06, A0A0G4GJ92, A0A0G4EN10, A0A0G4FC64, A0A0G4G604, A0A0G4H617,A0A0G4EE30, A0A0G4EMH2, A0A0G4EXD3, A0A0G4F467, A0A0G4ESG9, A0A0G4H5A7,A0A0G4H147, A0A0G4ELP5, A0A0G4EW80, A0A0G4EYN3, A0A0G4EVX9, A0A0G4G194,A0A0G4FYF0, A0A0G4ENT8, A0A0G4E913, A0A0G4EZ90, A0A0G4GDZ1, A0A0G4EV77,A0A0G4F2L7, A0A0G4FW07, A0A0G4END2, A0A0G4G025, A0A0G4EJ16, A0A0G4G3W1,A0A0G4ED81, A0A0G4EA18, A0A0G4GZE5, A0A0G4FZK6, A0A0G4F356, A0A0G4GY92,A0A0G4EP61, A0A0G4ERN6, A0A0G4F257, A0A0G4FG25, A0A0G4GJ87, A0A0G4GFW8,A0A0G4GN70, A0A0G4EGD8, A0A0G4GV35, A0A0G4EDK7, A0A0G4FDV3, A0A0G4EN36,A0A0G4FU39, A0A0G4G6I2, A0A0G4FAX9, Q948Y6, D8U662, D8UDJ2, D8UHS7,D8UHS1, D8U663, D8TZF2, D8TWV3, D8TZP2, D8ULZ4, D8U0L1, D8THZ2, D8U661,D8U9Q0, D8TUD4, D8TWS3, D8U5V3, D8TWS6, D8U656, D8UHS6, D8U0K8, D8TWV6,D8U3S1, A0A3Q7TWA6, A0A3Q7T0P7, A0A3Q7SNP7, A0A3Q7V334, A0A3Q7TKS7,A0A3Q7TAD2, A0A3Q7TW96, A0A3Q7UEY3, A0A0D0QEL7, A0A0D0PB00, A0A1M6EL45,A0A0C9S462, A0A0C9QPG3, A0A0C9RV88, A0A0C9RSU0, A0A0C9QPV3, A0A0C9RSN7,A0A0C9S6M8, A0A118E9A3, J9DND2, A0A3P7DL77, A0A1I8ELN8, A0A3P7EWD2,A0A1I8EZC2, J9ETT3, A0A118EY91, A0A118EL26, A0A1I8EZH7, A0A3P7GM02,J9DZA9, A0A3P7FT60, A0A3P7GCY4, J9E1R8, A0A1I8EFL2, A0A118EF35,A0A3P7EEQ9, A0A3P7FCC9, A0A3P7DVJ1, A0A3P7DV86, A0A1I8ET18, A0A3P7DDB0,A0A3P7DLR8, A0A1I8F0Y1, J9F728, J9F5K7, A0A1I8ELS4, A0A3P7EE66,A0A1I8EA12, J9ELM2, J9EVZ5, J9E6Y8, J9ESJ0, J9AHN9, A0A3P7GJ34,A0A1I8ESS3, J9E0L8, J9EHN5, A0A1I8ECU1, J9FCK3, A0A3P7FKH0, A0A3P7EG90,J9F005, J9FHZ7, J9F0L7, J9EDU4, A0A1I8EPI5, A0A1I8ENJ3, A0A1I8EHS2,A0A3P7E3Y0, A0A1I8ER89, J9AZF1, J9B8V2, A0A1L8G2F6, Q91691, A0A1L8GHB0,A0A1L8G2M6, A0A1L8GP52, Q7ZTN9, A0A1L8GTY1, A0A1L8GZD1, Q6GP14, Q6AZS7,P70006, F7EDW8, F6YRB8, F7AR31, Q91402, A0A3P5XFD2, A0A3B5KRY2,A0A3B5KXI9, A0A3B5KR76, A0A3B5MPU6, A0A3B5M999, A0A3B5KPF4, A0A3B5KR79,A0A3B5KQW4, A0A3B5MUP9, A0A3B5M3B3, A0A3B5MDS7, A0A3B5KJF0, A0A3B5MW25,M4ASA0, A0A3B5R264, M4AQQ5, A0A3B5R3X9, M4AAJ3, M3ZXK8, M3ZTS0, M3ZXL1,M3ZXJ9, M3ZQC7, A0A3B5PQ81, A0A439DFT7, A0A439CN67, A0A439CTF6,A0A2E1D5Y3, A0A2T6KMQ7, A0A116G2U0, A0A3L6D9L1, A0A3L6E7F7, A0A317YAC8,A0A3L6DRV9, A0A3L6E476, A0A317YET9, A0A3L6E218, A0A317YKF8, B6TY46,A0A317Y521, P17801, A0A1D6KQI4, C0P6F5, A0A1D6KH09, A0A096T7Z1,A0A1D6M0L4, A0A1D6LBB2, A0A1D6DXI3, A0A1D6F8W0, A0A1D6N9S7, A0A1D6DXH8,A0A1D6H9Q0, A0A1D6GN29, K7UZN2, A0A1D6IEQ3, A0A1D6P507, A0A1D6DXM7,A0A1D6J6V6, K7VD35, A0A1D6IAX9, C0P9N1, A0A1D6JF78, A0A1D6GA13,A0A1D6FGJ5, K7VRP4, A0A1D6DXM5, A0A1D6ML66, A0A1D6GA09, A0A1D6N9S3,A0A1D6HLB4, A0A1D6IER4, A0A1D6N9Q9, C0HFM8, A0A1D6KIF9, A0A1D6IEQ5,A0A1D6GA12, A0A1D6KAQ9, A0A1D6IEI3, A0A1D6FSS8, A0A1D6IEI1, A0A1D6N9R8,A0A1D6MFC2, A0A1D6M2E6, A0A1D6J6V7, A0A3L6E4L3, A0A1D6DXH6, A0A1D6J6V1,A0A1D6J6V2, A0A1D6M0N6, A0A1D6EWT3, B4G1J2, A0A1D6ITQ0, A0A1D6KQI3,A0A1D6KL97, A0A1D6N9R3, K7UIF8, A0A1D6M0N7, A0A1D6EB48, A0A1D6QAA8,A0A1D6P2B1, A0A1D6M0N8, A0A3L6DU79, A0A3L6EU45, A0A317Y2S5, B7ZXB0,A0A3L6FU88, A0A3L6DL74, B6U2B7, A0A3L6FAJ7, A0A3L6DY96, A0A1Q1B749,A0A3L6ET80, B6SWL2, A0A3L6GBB9, A0A3L6G7X6, A0A3L6E4K1, A0A3L6D8A7,A0A3L6DCB9, A0A3L6DDA9, B4F952, A0A3L6G155, O24571, A0A3L6G2G8, B6ST43,A0A3L6FWI8, A0A3L6EU60, B4FYC6, A0A1V0E7H4, B4F8X7, A0A1D6M0M0,A0A1D6KIH3, A0A1D6N9S8, A0A1D6G7A2, A0A1D6KNU3, A0A1D6P015, K7TKD2,C0P3V1, A0A3L6G196, A0A1D6DXM6, A0A1D6HWK7, A0A1D6DXF1, A0A1D6IEQ4,A0A1D6KII4, B4FB05, A0A1D6IBG7, A0A1D6DXI2, A0A1D6N9R2, K7UC64,A0A1D6G136, A0A1D6LHG9, A0A1D6Q5J8, A0A1D6DXH9, A0A1D6FSS9, A0A1D6DXI7,A0A1D6G137, A0A1D6IEI2, A0A1D6JTK4, A0A1D6JF77, K7U3E7, A0A1D6QHL5,A0A1D6HLB7, A0A1D6I5R1, A0A1D6GA10, A0A1D6LGF6, A0A1D6DXM4, A0A1D6EUL5,A0A317YAM4, A0A3L6ETW0, A0A3L6E3M3, O49974, A0A3L6FYL3, A0A3L6EW75,A0A317Y7G4, A0A317Y3N4, A0A3L6FI05, A0A3L6DN41, C0PE10, A0A3L6G6F6,A0A3L6G1E6, A0A3L6DU70, C0HEN9, A0A3L6G8Y0, A0A3L6FT98, A0A3L6EX22,A0A3L6EHP0, O82103, A0A3L6DLS3, B7ZXT8, A0A3L6F189, A0A3L6FL65,A0A3L6E7I6, B7ZWT1, A0A3L6G679, A0A3L6DII2, A0A3L6FF64, A0A3L6DKE6,A0A3L6FXI5, A0A3L6GCE3, A0A3L6FWN1, A0A3L6FGU1, A0A3L6GBY8, A0A3L6EFC7,A0A3L6FT74, A0A3L6EBY7, A0A317Y6J9, C0P3U3, A0AA1XIZ1, A0A0A1XS55,A0A0A1X650, A0A0A1XQ87, A0A0A1X1C0, A0A0A1XB00, A0A0A1X8W7, A0A0A1WII0,A0A0A1XIF3, A0A0A1WSF6, A0A2G1QQ59, A0A067RG78, A0A067RN91, A0A067R6A7,A0A067RBZ2, A0A067RIJ5, A0A0K9NV78, A0A0K9Q5Q1, A0A0K9PK14, A0A0K9P5Q8,A0A0K9NYD2, A0A0K9PEI3, A0A0K9PPY6, A0A0K9PXR7, A0A0K9PLY7, A0A0K9NWC4,A0A0K9PKC6, A0A0K9NQT5, A0A0K9P3S2, A0A0K9PQY0, A0A0K9PLW0, A0A0K9P3C4,A0A0K9PPJ9, A0A0K9P0C4, A0A0K9PY30, A0A0K9PNK6, A0A0K9PP88, A0A0K9P1W2,A0A0K9NS31, A0A0K9NWR2, A0A0K9NMN3, A0A0K9NJ97, A0A0K9PD87, A0A0K9NTS5,A0A0K9Q4R1, A0A0K9NIZ5, A0A0K9NQH7, A0A0K9PG70, A0A0K9NRX4, A0A0K9NV14,A0A0K9NLX9, A0A0K9P5H7, A0A0K9NPE2, A0A0K9P819, A0A0K9PRP8, A0A0K9P5Q0,A0A0K9PM56, A0A0F4GX70, A0A0F4GNN3, A0A0F4GDY3, A0A0F4G7R0, A0A0F4GJL4,A0A0F4G525, A0A0F4GKZ5, A0A0F4GK64, A0A0F4GK12, A0A0F4GVA7, A0A0F4GTQ5,A0A0F4GJJ0, A0A0F4GPQ0, A0A0F4GLI2, F9X4T1, F9XHT4, F9XH72, F9XJG6,F9XDZ3, F9X146, F9XK84, F9XCF6, F9XP87, F9X6W1, F9XFV9, F9XM39, F9XAK9,F9XNE3, A0A1Y6LP08, A0A1Y6LZ79, A0A1Y6LY30, A0A1Y6LT89, A0A1Y6L814,A0A1Y6LQH5, A0A1Y6LQU6, A0A1Y6L5Q9, A0A1Y6LXG6, A0A1Y6LN68, A0A1Y6LFZ2,A0A1Y6LBN0, A0A1Y6LDV9, A0A1Y6L8C9, A0A1Y6LRA7, A0A2H1FJ88, A0A2H1GP22,A0A2H1H488, A0A2H1FZK2, A0A2H1H533, A0A2H1FLY6, A0A2H1H4S8, A0A2H1GT42,A0A2H1GHG1, A0A2H1H5M8, A0A2H1GTE8, A0A2H1FQ02, A0A2H1G5G9, A0A2H1GXW6,A0A2H1GZK0, A0A2H1GNU0, A0A2H1GST3, A0A2H1H7P5, A0A1X7RYL6, A0A1X7RF14,A0A1X7RL97, A0A1X7RUL5, A0A1X7S239, A0A1X7RV33, A0A1X7RNL6, A0A1X7RY43,A0A1X7S9D0, A0A1X7S2M2, A0A1X7S7L9, A0A1X7RBY3, A0A1X7S0P9, andA0A1X7RID6.

What is claimed is:
 1. A method for screening for an immunoregulatoryprotein comprising: assessing the sequence of a candidate protein, anddetermining that the candidate protein is an immunoregulatory proteinwhen at least one Plasminogen Apple Nematode (PAN) domain is found inthe sequence.
 2. The method for claim 1, wherein the PAN domain has aconsensus sequence as shown in SEQ ID NO:
 23. 3. A method for screeningfor a therapeutic compound targeting a PAN domain in a protein,comprising: contacting the protein comprising the PAN domain with acandidate therapeutic compound, and assessing whether the compound bindsto the PAN domain.
 4. The method of claim 3, wherein the PANdomain-containing protein is selected from proteins listed in List
 1. 5.A method for screening for a MET signaling inhibitor, comprisingexpressing a c-MET receptor on the surface of a cell; incubating thecell with Hepatocyte Growth Factor (HGF) in the presence of a candidateinhibitor of PAN domain interactions; and determining that the candidateinhibitor is an inhibitor of c-MET signaling if the interaction withc-MET and HGF is inhibited.
 6. The method of claim 5, wherein thecandidate inhibitor of PAN domain interactions is a peptide comprising aconsensus sequence as shown in SEQ ID NO:
 23. 7. The method of claim 5,wherein the candidate inhibitor of PAN domain interactions is a smallmolecule.
 8. A method for enhancing immune response to a pathogen in aplant comprising inactivating a gene encoding a PAN domain-containingprotein in the plant.
 9. The method of claim 8, wherein the inactivatingis achieved by introducing a non-silent mutation in the gene at aposition encoding a conserved cysteine residue of the PAN domain. 10.The method of claim 8, wherein the PAN domain-containing protein isselected from plant G-type receptor-like protein kinases.
 11. The methodof claim 9, wherein the conserved cysteine residue is selected from aresidue equivalent to a cysteine at position 1, 32, 36, 40, 42, or 57 ofSEQ ID NO:
 25. 12. The method of claim 9, wherein the non-silentmutation is a nonconservative mutation.
 13. The method of claim 12,wherein the nonconservative mutation is a cysteine to alanine mutation.14. The method of claim 8, wherein the inactivating of the gene encodinga PAN domain-containing protein is achieved by introducing an exogenousnucleic acid inhibitor of the gene to the plant.
 15. The method of claim14, wherein the nucleic acid inhibitor is selected from the groupconsisting of an antisense RNA, a small interfering RNA, an RNAi, amicroRNA, an artificial microRNA, and a ribozyme.
 16. The method ofclaim 8, wherein the inactivating of the selected gene is achieved bygenome editing, which is achieved by a method selected from the groupconsisting of CRISPR/Cas system, Cre/Lox system, TALEN system, ZFNssystem and homologous recombination.
 17. The method of claim 16, whereinthe CRISPR-mediated genome editing comprises introducing into the planta first nucleic acid encoding a Cas9 nuclease, a second nucleic acidcomprising a guide RNA (gRNA), wherein said gRNA is specific to the geneencoding a PAN domain containing protein.
 18. The method of claim 16,wherein the CRISPR-mediated genome editing comprises introducing intothe plant a first nucleic acid encoding a Cas9 nuclease, a secondnucleic acid comprising a guide RNA (gRNA), wherein said gRNA isspecific to the gene encoding a PAN domain containing protein gene, anda third nucleic acid comprising a template for homologous recombination.19. The method of claim 8, wherein the pathogen is selected from abacterium, a virus or a fungus.
 20. A genetically engineered plant,wherein an endogenous gene encoding a PAN domain-containing protein hasbeen inactivated as a result of a genetic modification.
 21. Thegenetically engineered plant of claim 20, wherein the inactivating isachieved by introducing a non-silent mutation in the gene at a residueencoding a conserved cysteine residue of the PAN domain.
 22. Thegenetically engineered plant of claim 20, wherein the PANdomain-containing protein is selected from G-type receptor-like proteinkinases.
 23. The genetically engineered plant of claim 21, wherein theconserved cysteine residue is selected from a residue equivalent to acysteine at position 1, 32, 36, 40, 42, or 57 of SEQ ID NO:
 25. 24. Thegenetically engineered plant of claim 21, wherein the non-silentmutation is a nonconservative mutation.
 25. The genetically engineeredplant of claim 24, wherein the nonconservative mutation is a cysteine toalanine mutation.
 26. A method for preventing cell division of a humancell comprising inactivating a gene encoding a PAN domain containingprotein in the human cell.
 27. The method of claim 26, wherein theinactivating is achieved by introducing a non-silent mutation in thegene at a residue encoding a conserved cysteine residue of the PANdomain.
 28. The method of claim 26, wherein the PAN domain containingprotein gene is Hepatocyte Growth Factor (HGF).
 29. The method of claim27, wherein the conserved cysteine residue is selected from a residueequivalent to a cysteine at position 34, 38, 48, or 60 of SEQ ID NO: 32.30. The method of claim 27, wherein the non-silent mutation is anonconservative mutation.
 31. The method of claim 30, wherein thenonconservative mutation is a cysteine to alanine mutation.
 32. Themethod of claim 26, wherein the inactivating of the gene encoding a PANdomain-containing protein is achieved by introducing an exogenousnucleic acid inhibitor of the gene to the cancer cell.
 33. The method ofclaim 32, wherein the nucleic acid inhibitor is selected from the groupconsisting of an antisense RNA, a small interfering RNA, an RNAi, amicroRNA, an artificial microRNA, and a ribozyme.
 34. The method ofclaim 26, wherein the inactivating of the gene encoding a PANdomain-containing protein is achieved by genome editing, which isachieved by a method selected from the group consisting of CRISPR/Cassystem, Cre/Lox system, TALEN system, ZFNs system and homologousrecombination.
 35. The method of claim 34, wherein the CRISPR-mediatedgenome editing comprises introducing into the cancer cell a firstnucleic acid encoding a Cas9 nuclease, and a second nucleic acidcomprising a guide RNA (gRNA), wherein said gRNA is specific to the geneencoding a PAN domain containing protein.
 36. The method of claim 34,wherein the CRISPR-mediated genome editing comprises introducing intothe cancer cell a first nucleic acid encoding a Cas9 nuclease, a secondnucleic acid comprising a guide RNA (gRNA), wherein said gRNA isspecific to the gene encoding a PAN domain containing protein, and athird nucleic acid comprising a template for homologous recombination.37. A method for improving in vitro fertilization (IVF) efficiency in anon-human subject suffering from infertility comprising: determining thesequence of a gene that encodes a PAN domain-containing protein, andobtaining an ovum or a sperm from the subject when a mutation is foundin a conserved cysteine of the PAN domain of the PAN domain-containingprotein, correcting the mutation in the PAN domain-containing protein inthe ovum or the sperm.
 38. The method of claim 37, wherein the PANdomain-containing protein gene is a Zona Pellicuda(ZP) protein.
 39. Themethod of claim 37, wherein the conserved cysteine residue is selectedfrom a residue equivalent to a cysteine residue in SEQ ID NO:
 23. 40.The method of claim 37, wherein the correcting of the PAN domain isachieved by genome editing, which is achieved by a method selected fromthe group consisting of CRISPR/Cas system, Cre/Lox system, TALEN system,ZFNs system and homologous recombination.
 41. The method of claim 40,wherein the CRISPR-mediated genome editing comprises introducing intothe ovum or the sperm a first nucleic acid encoding a Cas9 nuclease, asecond nucleic acid comprising a guide RNA (gRNA), wherein said gRNA isspecific to the gene encoding a PAN domain-containing protein, and athird nucleic acid comprising a template for homologous recombinationthat corrects the mutated residue to cysteine.
 42. The method of claim37, wherein the ovum or the sperm is from a domesticated animal.
 43. Amethod for preventing pregnancy or implantation of a fetus in anon-human subject comprising inactivating a gene encoding a PANdomain-containing protein in an ovum or a sperm.
 44. The method of claim43, wherein the inactivating is achieved by introducing a non-silentmutation in the gene at a residue encoding a conserved cysteine residueof the PAN domain.
 45. The method of claim 43, wherein the PAN domaincontaining protein gene is a Zona Pellicuda protein.
 46. The method ofclaim 44, wherein the conserved cysteine residue is selected from aresidue equivalent to a cysteine residue in SEQ ID NO:
 23. 47. Themethod of claim 43, wherein the non-silent mutation is a nonconservativemutation.
 48. The method of claim 47, wherein the nonconservativemutation is a cysteine to alanine mutation.
 49. The method of claim 43,wherein the inactivating of the gene encoding a PAN domain-containingprotein is achieved by introducing an exogenous nucleic acid inhibitorof the gene to the ovum or the sperm.
 50. The method of claim 49,wherein the nucleic acid inhibitor is selected from the group consistingof an antisense RNA, a small interfering RNA, an RNAi, a microRNA, anartificial microRNA, and a ribozyme.
 51. The method of claim 43, whereinthe inactivating of the gene encoding a PAN domain-containing protein isachieved by genome editing, which is achieved by a method selected fromthe group consisting of CRISPR/Cas system, Cre/Lox system, TALEN system,ZFNs system and homologous recombination.
 52. The method of claim 51,wherein the CRISPR-mediated genome editing comprises introducing intothe ovum or the sperm a first nucleic acid encoding a Cas9 nuclease, asecond nucleic acid comprising a guide RNA (gRNA), wherein said gRNA isspecific to the gene encoding a PAN domain-containing protein.
 53. Themethod of claim 51, wherein the CRISPR-mediated genome editing comprisesintroducing into the ovum or the sperm a first nucleic acid encoding aCas9 nuclease, a second nucleic acid comprising a guide RNA (gRNA),wherein said gRNA is specific to the selected gene, and a third nucleicacid comprising a template for homologous recombination.
 54. The methodof claim 43, wherein the ovum or the sperm is from a domesticatedanimal.
 55. A method for screening for an oncoprotein protein in amammalian cell comprising: assessing the sequence of a candidateprotein, and determining that the candidate protein is an oncoproteinwhen at least one Plasminogen Apple Nematode (PAN) domain is found inthe sequence.
 56. The method for claim 55, wherein the PAN domain has aconsensus sequence as shown in SEQ ID NO:
 23. 57. A method forinactivating a PAN domain-containing protein comprising introducing anon-silent mutation in the protein at a residue encoding a conservedcysteine residue of the PAN domain.
 58. The method of claim 57, whereinthe PAN domain-containing protein is selected from proteins listed inList
 1. 59. The method of claim 57, wherein the conserved cysteineresidue is selected from a residue equivalent to a cysteine residue inSEQ ID NO: 23.